A method of increasing photosynthetic capacity in a plant by use of a nadph or nadh water- forming oxidase

Abstract

The present invention relates to polynucleotides comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The invention also relates to methods for increasing the growth and yield of plants.

Description

[0001]METHOD Field of the Invention The present invention relates to polynucleotides comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The invention also relates to methods for increasing the growth and yield of plants. Background of the Invention Photosynthesis Increasing human population and climate change place significant pressure on agricultural production, such that crop yields need to be substantially increased by 2050 to meet expected demand. This increased yield must be achieved using sustainable approaches to avoid exacerbating climate change and accelerating biodiversity loss through expansion of agriculture. Enhancing photosynthesis is regarded as one of the most promising avenues for increasing crop yield. In photosynthesis, ribulose-1,5-bisphosphate carboxylase / oxygenase (rubisco) is the enzyme that converts atmospheric CO2into the sugars that sustain plant growth. The rate at which rubisco catalyses CO2fixation determines the maximum rate of biomass accumulation (and hence growth and yield) in plants. However, rubisco also catalyses a competing reaction with O2which depletes photosynthetic metabolite pools and incurs an energetic and resource cost in a process known as photorespiration. The rate at which rubisco fixes CO2and makes sugar, or fixes O2and loses energy, is dependent on the concentration of these two gases in the chloroplast where rubisco is located. In normal field conditions, photorespiration can cause a decrease in crop yield by up to 36% resulting in millions of tons of lost crop productivity annually. Moreover, as photorespiration increases with increased temperature, climate change is predicted to exacerbate crop losses through increased rates of photorespiration. Thus, there is substantial interest in methods to reduce the occurrence of photorespiration in order to improve plant growth and crop yield, and by extension, help safeguard plants against future temperature rises. Previous attempts to mitigate yield loss from photorespiration have focussed on the introduction of photorespiratory bypasses (Kebeish et al., 2007 Nature Biotechnology 25(5):593-9, Maier et al., 2012 Frontiers in Plant Science 28;3:38, South et al., 2019 Science 4;363(6422) Shen et al., 2019 Molecular Plant 12: 199-214, Basler et al. 2016 Frontiers in Bioengineering and Biotechnology 4:31, Maurino 2019 Frontiers in Bioengineering and Biotechnology 47:61805-1813). Each of these approaches attempt to provide a more energy efficient route to the recovery of photorespired CO2either by lowering the ATP and NADPH cost to convert 2-phosphoglycolate to 3-phosphoglycerate, or, by releasing photorespired CO2in close proximity to rubisco. Although, many attempts have been made to decrease the impact of photorespiration by engineering alternative less costly pathways, no-one has yet managed to decrease the occurrence of photorespiration through alteration of the relative concentration of CO2and O2in the chloroplast where rubisco is located. The present invention provides a novel and innovative solution to alter the relative abundance of O2and CO2around rubisco in plants to enhance growth and yield. Stomata Stomata mediate the exchange of gaseous CO2and water vapour between plants and their external environment. Specifically, CO2provides the primary substrate of photosynthesis and its uptake is thereby required to fuel plant growth. In contrast, loss of water vapour is integral to the transpiration stream which helps regulate internal water status, temperature, and nutrient uptake. As both CO2and H2O gases share a single diffusion path but in opposite directions, controlling flux along this path is essential for balancing the physiological demands of the individual. Consequently, optimizing the distribution and function of stomata is a central component of maximizing the productivity of plants in terrestrial habitats. Given their role at the interface between plants and their environment, stomata are capable of modulating their diffusive conductance in response to diverse stimuli including light (quality and quantity), humidity, temperature, soil water availability, and atmospheric CO2. Using these signals alongside natural circadian rhythms, stomata open to promote CO2fixation during the day and close at night or under adverse conditions to limit excessive water loss. In addition to this dynamic behaviour, stomata also exhibit remarkable developmental plasticity in response to diverse environmental changes. For instance, the number and distribution of stomata on leaf abaxial and adaxial surfaces can vary both between species, as well as between individuals of the same species depending on light availability. Stomatal density also exhibits remarkable plasticity and varies between individuals depending on soil water availability, temperature, ambient CO2concentration, and relative air humidity. These environmentally-induced changes in density are also associated with secondary adjustments in stomatal size (such that higher densities of stomata are smaller and vice versa), although density always takes precedence over size as the predominant anatomical constraint on leaf gaseous conductance. Thus, both dynamic and developmental changes in stomata play important roles in the growth and environmental adaptation of plants. The considerable plasticity of stomatal form and function, coupled with the importance of stomata in regulating plant growth and environmental interactions, have together inspired multiple attempts to alter their properties for crop improvement. These successes date back to the pioneering work of Farquhar and Richards in the 1980s (Farquhar GD. and Richards RA. 1984 Australian Journal of Plant Physiology, 11(6), 539– 552) who used stable carbon isotope ratios to screen for enhanced water use efficiency in wheat. Subsequently, efforts have expanded to include a range of forward genetic approaches which have manipulated stomatal distribution, as well as the mechanical, transport, and metabolic properties of stomatal guard cells. Of these approaches, altering stomatal density has received the most attention with a wide range of mutants exhibiting both increases and decreases in stomatal numbers across a diverse array of plant species. A common theme in approaches which have altered stomatal densities has been the genetic manipulation of the expression levels of stomatal development genes. These include the basic helix-loop-helix transcription factors SPEECHLESS (SPCH) (Gudesblat G.E. et al. 2012 Nature Cell Biology 14, 548–554), MUTE (Pillitteri, LJ. et al. 2007 Nature 445, 501–505), and FAMA (Bergmann DC. et al. 2004 Science 304, 1494–1497) which respectively regulate the initiation, proliferation, and differentiation stages of the stomatal lineage. Engineering success has also been achieved from targeting other important components of stomatal development including the EPIDERMAL PATTERNING FACTOR family of signalling peptides alongside their receptor components TOO MANY MOUTHS and the ERECTA protein kinases, stomatal density and distribution 1 (SDD1) and its respective interactor components, as well as a host of other genes involved in hormone signalling and plant developmental processes. However, the molecular and biochemical mechanisms that link changes in gene networks to changes in environmental and physiological cues remain less well understood. As such, there has been comparatively little focus on efforts to manipulate the stomatal density of plants via metabolic engineering. Water-forming NADH and NADPH oxidases Water-forming NADH or NADPH oxidases are enzymes that can oxidize NADH or NADPH to NAD+ or NADP+, respectively. They function by reducing molecular oxygen by a four-electron transfer from a reducing equivalent in the presence of protons to form water and an electron acceptor (Petschacher B et. al. Computational and Structural Biotechnology Journal. 2014 Feb 26;9:e201402005. doi: 10.5936 / csbj.201402005). Different isoforms of water-forming NADH or NADPH oxidases can selectively use NADH or NADPH or can use both (Gao H, et al. International Journal of Biological Macromolecules 2019. 15;123:629-636. doi: 10.1016 / j.ijbiomac.2018.11.096). As these enzymes use oxygen as substrate and produce water as a by-product they are frequently used for cofactor regeneration in biotechnological applications. To date, several water-forming NADH or NADPH oxidases have been identified in a diverse array of organisms ranging from bacteria (Higuchi M, et al 1993 The Journal of General Microbiology. 139, 2343–2351), to archaea (Ward D.E., 2001 FEBS J. 268:5816– 5823), to eukaryotes (Brown D.M., et al 1996 European journal of biochemistry, 241(1), 155-161). In addition to naturally occurring enzyme variants, water-forming NADH or NADPH oxidase enzymes have also been the subject of enzyme engineering efforts (Petschacher B, et al. 2014 Computational and structural biotechnology journal, 9(14), p.e201402005) to alter their substrate and / or co-factor specificity. Thus, there are a wide variety of water-forming NADH or NADPH oxidases (natural or engineered) from a wide variety of organisms that are known in the art. The invention particularly concerns water- forming oxidases that reduce molecular oxygen to form water through the conversion of NADPH or NADH to NADP or NAD, respectively. The invention provides a new polynucleotide comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. Plants may be genetically engineered to comprise the polynucleotide of the invention, which may in turn drive enhanced growth and biomass production. The polynucleotide of the invention may particularly drive enhanced plant growth and biomass production by modulating the relative abundance of O2and CO2in proximity to rubisco. The polynucleotide of the invention may drive enhanced plant growth and biomass production by decreasing stomatal density and by enhancing the plant water use efficiency. Accordingly, the invention has the potential to positively impact global crop yield production. Summary of the Invention The inventors have devised a novel approach for enhancing plant growth and yield. This is achieved through the engineering of plants to contain a polynucleotide comprising a promoter element operatively linked to a nucleotide sequence that encodes a water- forming oxidase. The polynucleotide may advantageously enhance plant growth and yield by altering the relative concentration of CO2and O2in proximity to rubisco in the chloroplast, thereby reducing the occurrence of photorespiration. The invention may be particularly advantageous in numerous applications including, but not limited to, industrial biotechnology (wherein enhanced growth and / or yield would result in enhanced production of proteins, peptides, metabolites, molecules, compounds, and the like), and in food, feed, biomass and biofuel production (wherein enhanced growth and / or yield would result in enhanced production of food, feed, biomass or biofuel). The invention shows that the expression of one or more water-forming NADH or NADPH oxidases in plant cells results in enhanced plant growth and biomass production. The present invention also particularly demonstrates that multiple different natural or engineered water-forming oxidases (e.g. NADH or NADPH) genes from different species can provide this function. The present invention further demonstrates that this function can be provided by these proteins when expressed in their unmodified form, and / or as fusion proteins, and / or as proteins that are targeted to specific subcellular compartments, and / or as proteins that are anchored to cellular membranes. The present invention also demonstrates that the protein(s) in various compositional forms described above can also be expressed in plant cells using promoters that are ubiquitously active in every tissue in the plant, as well as those that are exclusively expressed in photosynthetically active cells using cell and / or tissue specific promoters. The invention provides a polynucleotide comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The invention also provides a vector comprising a polynucleotide of the invention. The invention additionally provides a composition for transforming plant cells, the composition comprising a polynucleotide of the invention and / or a vector of the invention, preferably wherein the composition comprises a microparticle complexed with the polynucleotide and or the vector. The invention further provides a cell comprising a polynucleotide of the invention, or comprising a vector of the invention. The invention also provides a plant or part thereof comprising: (i) a cell of the invention; or (ii) a cell comprising a polynucleotide which comprises a promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The invention additionally provides a method for increasing photosynthetic capacity of a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one mesophyll cell of the plant, thereby increasing photosynthetic capacity of the plant. The invention additionally provides a method for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one cell of a plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the stomatal cell is a stomatal progenitor cell. The invention further provides a plant part, plant tissue, plant organ, plant cell, plant protoplast, embryo, callus culture, pollen grain or seed derived from a plant of the invention, or derived from a plant produced by a method of the invention, optionally wherein the plant part comprises a nucleic acid sequence corresponding to the water- forming oxidase as defined herein. The invention further provides a use of a water-forming oxidase for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the use comprises cultivating a plant comprising a nucleotide sequence corresponding to the water-forming oxidase defined according to the invention. Brief Description of the Figures Figure 1 shows simplified schematics of the genetic constructs used for expression of water-forming oxidase genes in this invention. A) The expression cassette for expressing water-forming oxidase genes fused at their C-terminus to GFP under the control of the CaMV 35S promoter. B) As in A) but with an N-terminal fusion protein (NTFP). C) The expression cassette for expressing water-forming oxidase genes under the control of the chlorophyll a / b-binding protein 3 (CAB3) promoter. D) As in C but with the addition of an NTFP. All expression cassettes include the nopaline synthase terminator (NOSt). Figure 2 shows images of plant cells (protoplasts) expressing water-forming oxidase genes fused to GFP at their C-termini. The top row shows a free GFP control. The second row shows images of a protoplast expressing the LbNOX water-forming oxidase that is translationally fused in-frame at its C-terminus to GFP. The third row shows images of a protoplast expressing an SmNOX water-forming oxidase that is targeted to the chloroplast intermembrane space by translationally fusing the SmNOX gene to outer envelope protein 9 at its N-terminus and GFP at its C-terminus. The fourth row shows images of a protoplast expressing an SmNOX water-forming oxidase that is targeted to the chloroplast stroma by translationally fusing the SmNOX gene to the oxygen evolving protein 16 chloroplast target peptide sequence at its N-terminus and GFP at its C-terminus. The fifth row shows images of a protoplast expressing an SmNOX water-forming oxidase that is targeted to the chloroplast stroma by translationally fusing the SmNOX gene to the rubisco small subunit protein sequence at its N-terminus and GFP at its C-terminus. Figure 3 shows the impact of the expression of water-forming oxidase genes on plant growth and yield. A) The growth rate of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). B) The visible rosette area at day 20 of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). C) The inflorescence height at day 32 of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). D) The time to flowering of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). Letters above box plots indicate significant differences between groups (p < 0.05) from one-way analysis of variance with Tukey test for multiple comparison. Figure 4 shows the impact of the expression of water-forming oxidase genes on stomatal density, stomatal conductance, and photosynthetic water-use efficiency. A) The stomatal density (count mm−2) on the abaxial surface from mature rosette leaves of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). B) The light-saturated stomatal conductance (gs sat,mol m−2 s−1) of mature rosette leaves of plant lines expressing water-forming oxidases compared to non-modified control plants (WT). C) The light-saturated intrinsic water-use efficiency (iWUEsat, μmol mol−1) of mature rosette leaves of plant lines expressing water-forming oxidases compared to non- modified control plants (WT). Differences between transgenic plants and WT are assessed by Fisher LSD post-hoc analysis following a two-way ANOVA, where letters above each box represent statistically significant differences in mean values (p ≤ 0.05). Brief Description of the Sequences SEQ ID NO: 1 – The nucleotide sequence of Arabidopsis thaliana CAB3 promoter TCTGAAGCTCGTAACATTGGCTCATACGATATCTGGATAACAATATATCACATTGCTCTGATACCATATTAAA ATCACATCCACGCATTGAATGGACTGATCATATATCTTACATATTAGTTAAAATCCATTGTCGTGCGAGAGAT TGCCTTCCGTGACATCCTCTGTGGACCAGGTTCGCTTGTCACACTAGCTATAATTGGTGAACACATGATAACA TATATGTTTGGAGCATAGAAGAGCTAGCGCCTGTGTCATTGGTGTGTGGTATCGAAAGAACAAGAGAATAGAA CAGGAGAACATGAATATAGCTAGGTTTATTCATTTTCACCCCAAAGCTTAGAAATTGCGTTCCAAAGAGTGGG TGAATTCATGTGTGAGGGCAATTAGTGATTGTAAAAATAAAATTGTGTTTTGTAAAAAACTTTTACTGTCGAA ATTATTTAGGGTGATGAAAAAATCAGTAAACTACGAATGATAGCTTAAAGAGTTTCTATCAAAGTGATTGAGG AATAGTTTGTTGCAAATTAAACCTCTAACAAAATGTTTTCTGTTGTGGTTTTTCATCTCTACAAATTTTGAAT TTTATGATGAATTAGAAAGATAGAATGAGTTACTTTAGATTTTAAAAGGTTGTTCAAGTTTACAAAACAGATT ACTAGAATCATGATTAAAAATTTACAAGCTACATATTGTCTAAACCAATGATGTTGAACATACCAGATGATAG TTTTTCAGTGTTTGAACAATCAATTGGATAGTTTTTATGTTTCTGCAAAATATGCAAATAATCAGTGTTTTTG AGTCTTTGCATTTTGATTTAAAAGCAAAAACAACTGAGTTTCAAGGTTAAATTAATTACATTATTCATGAGAT TTATCAGGTTAGTGGATAAACTGACAATGGAATCAATGTTATTGTAAATTGGTAGTGATGTTGGACTTCTAAT GTTACTCTCTATGATGTTTCGGTCATCAATATCACACTATCTTTACTTTTATTTAAAGGAAAGATCACACAAA TAAGTTATCTCTATTCAGAACTATTAAGCTGCTTCCAAAAGACTTGCAACATGTGGACTCGAAATGCTTTGGC TGCAATGAAAAAATCATAGCAAAAGCTAGTGGACTAGAGACTGCCACATAAGAATAGTAAACGTTAAAACCAA AATCTCAAAAATCCAATGAGTAAAGAGATATAGATTACTTCATAGATAACAAACGTTACTCGCAATTTTCCTA TATAATCCAACCCTACCTAACCATTTTCAATCACTCTCACTCACAAGTTAGTCACCAAAAAAAAAAAAAAACA CAAAAAGTTTC SEQ ID NO: 2 – The nucleotide sequence of CaMV 35S promoter GTCAACATGGTGGAGCACGACACTCTGGTCTACTCCAAAAATGTCAAAGATACAGTCTCAGAAGATCAAAGGG CTATTGAGACTTTTCAACAAAGGATAATTTCGGGAAACCTCCTCGGATTCCATTGCCCAGCTATCTGTCACTT CATCGAAAGGACAGTAGAAAAGGAAGGTGGCTCCTACAAATGCCATCATTGCGATAAAGGAAAGGCTATCATT CAAGATCTCTCTGCCGACAGTGGTCCCAAAGATGGACCCCCACCCACGAGGAGCATCGTGGAAAAAGAAGAGG TTCCAACCACGTCTACAAAGCAAGTGGATTGATGTGACATCTCCACTGACGTAAGGGATGACGCACAATCCCA CTATCCTTCGCAAGACCCTTCCTCTATATAAGGAAGTTCATTTCATTTGGAGAGGACACGC SEQ ID NO: 3 - The nucleotide sequence of Agrobacterium tumefaciens nos terminator including 3'UTR GTCAAGCAGATCGTTCAAACATTTGGCAATAAAGTTTCTTAAGATTGAATCCTGTTGCCGGTCTTGCGATGAT TATCATATAATTTCTGTTGAATTACGTTAAGCATGTAATAATTAACATGTAATGCATGACGTTATTTATGAGA TGGGTTTTTATGATTAGAGTCCCGCAATTATACATTTAATACGCGATAGAAAACAAAATATAGCGCGCAAACT AGGATAAATTATCGCGCGCGGTGTCATCTATGTTACTAGATCGA SEQ ID NO: 4 - The codon optimised nucleotide sequence of monomeric enhanced GFP ATGGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACG GCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGCGATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTG CACCACCGGCAAGCTGCCCGTGCCCTGGCCCACCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGC CGCTACCCCGACCACATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCA CCATCTTCTTCAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAA CCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTAC AACAGCCACAACGTCTATATCATGGCCGACAAGCAGAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACA ACATCGAGGACGGCAGCGTGCAGCTCGCCGACCACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCT GCTGCCCGACAACCACTACCTGAGTACTCAGTCCAAGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATG GTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 5 - The amino acid sequence of monomeric enhanced GFP MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFS RYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNY NSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHM VLLEFVTAAGITLGMDELYK SEQ ID NO: 6 - The codon optimised nucleotide sequence of Arabidopsis thaliana rubisco small subunit ATGGCTTCTTCTATGCTGTCCAGCGCTACTATGGTGGCATCTCCCGCACAGGCTACCATGGTCGCTCCCTTCA ATGGCTTGAAATCTTCCGCTGCCTTCCCCGCAACACGCAAGGCGAACAATGATATCACTAGCATTACCTCTAA CGGAGGTCGTGTCAATTGTATGCAGGTGTGGCCTCCCATCGGTAAAAAGAAGTTCGAAACCCTGAGCTACCTG CCTGACCTGACTGACTCTGAGCTGGCAAAGGAGGTTGACTATCTGATCCGTAACAAGTGGATTCCCTGCGTTG AGTTTGAGCTCGAGCATGGGTTCGTTTACCGTGAGCACGGAAACTCTCCCGGATATTACGACGGTCGTTACTG GACCATGTGGAAACTGCCACTTTTCGGTTGCACTGATTCTGCACAGGTCCTTAAGGAAGTTGAGGAATGCAAA AAGGAGTATCCAAACGCATTCATCCGTATCATTGGATTTGACAACACTCGCCAGGTGCAATGCATTTCATTCA TCGCCTACAAGCCCCCTTCGTTTACCGGTTAG SEQ ID NO: 7 - The amino acid sequence of Arabidopsis thaliana rubisco small subunit MASSMLSSATMVASPAQATMVAPFNGLKSSAAFPATRKANNDITSITSNGGRVNCMQVWPPIGKKKFETLSYL PDLTDSELAKEVDYLIRNKWIPCVEFELEHGFVYREHGNSPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECK KEYPNAFIRIIGFDNTRQVQCISFIAYKPPSFTG SEQ ID NO: 8 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide ATGGCTTCTATGGGCGGACTGCACGGGGCCTCCCCCGCAGTCTTGGAGGGAAGCCTGAAGATCAACGGTTCTT CACGTCTGAATGGATCTGGACGCGTGGCTGTTGCACAGCGCTCTCGTCTGGTTGTGCGTGCTCAGCAGTCGGA GGAAACCTCTCGTCGTAGCGTCATTGGTCTTGTCGCAGCGGGTCTGGCAGGTGGTTCTTTCGTTCAAGCTGTG CTGGCTGACGCAATCAGCATTAAAGTTGGACCCCCTCCCGCC SEQ ID NO: 9 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide MASMGGLHGASPAVLEGSLKINGSSRLNGSGRVAVAQRSRLVVRAQQSEETSRRSVIGLVAAGLAGGSFVQAV LADAISIKVGPPPA SEQ ID NO: 10 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide ATGGCCTACAGCGCTTGTTTCCTGCACCAGAGCGCTCTGGCTTCTTCTGCTGCACGTTCTTCCTCCTCATCTT CTTCCCAGCGTCACGTGTCTCTTTCTAAGCCCGTCCAGATTATCTGCAAAGCACAACAGAGCCATGAGGACGA TAACTCTGCAGTTTCTCGTCGCCTGGCATTGACCCTGCTGGTTGGAGCGGCAGCTGTCGGTTCAAAGGTTAGC CCTGCAGACGCC SEQ ID NO: 11 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVS PADA SEQ ID NO: 12 - The codon optimised nucleotide sequence of Arabidopsis thaliana outer envelope protein 9 ATGGGTAACGAAACCAAGACTAATGGGGGTCCTGCTAGCATGGCTGGAGGCGGAGGTTTCCGTGCAAAAATGG AGCATTACGTTTACTCTGGTGAAAAGAAGCACGTCCTTGTCGGTATCGGAATCGTTACCATTATTTTTGGAGT GCCCTGGTATCTGATGACTCAGGGATCTAAACACCAGAGCCACCAAGACTATATGGATAAGGCCGACAAGGCA CGCAAGGCTCGTCTGTCCTCTTCATCTTCTGCAAACAAATAG SEQ ID NO: 13 - The amino acid sequence of Arabidopsis thaliana outer envelope protein 9 MGNETKTNGGPASMAGGGGFRAKMEHYVYSGEKKHVLVGIGIVTIIFGVPWYLMTQGSKHQSHQDYMDKADKA RKARLSSSSSANK SEQ ID NO: 14 - The codon optimised nucleotide sequence of Lactobacillus brevis NAD(P)H oxidase ATGAAGGTGACTGTCGTGGGCTGCACACACGCTGGTACGTTCGCAATTAAACAGATTCTGGCAGAGCACCCCG ATGCGGAGGTTACCGTTTACGAGCGTAATGATGTCATCTCGTTCCTGTCGTGTGGTATCGCACTGTACCTGGG TGGAAAGGTCGCAGACCCTCAGGGACTGTTCTACAGCTCTCCCGAGGAACTGCAGAAGCTGGGAGCAAACGTG CAGATGAACCACAACGTCCTGGCAATCGATCCCGACCAGAAAACTGTGACTGTTGAGGATCTGACCAACCACG CTCAAACCACTGAGTCTTACGATAAGCTGGTCATGACTTCTGGGTCCTGGCCTATTGTTCCAAAGATCCCCGG AATCGATAGCGACCGCGTGAAGCTGTGCAAGAATTGGGCGCACGCACAAGCCCTGATTGAGGACGCAAAGGAA GCAAAGCGTATTACTGTTATCGGTGCTGGTTATATCGGAGCAGAGCTCGCCGAGGCTTATTCTACCACTGGTC ATGACGTTACCCTTATTGACGCTATGGCTCGCGTTATGCCCAAGTATTTCGACGCTGACTTCACTGACGTCAT TGAACAGGACTACCGTGATCACGGTGTTCAGCTGGCACTGGGAGAGACTGTTGAATCTTTTACCGACTCTGCC ACCGGTTTGACCATTAAAACTGACAAGAATTCCTATGAGACTGATCTGGCCATTCTGTGCATTGGTTTCCGTC CCAACACTGACCTGCTTAAAGGTAAAGTTGACATGGCTCCCAATGGAGCAATAATCACCGACGACTACATGCG CTCTAGCAATCCCGACATCTTCGCCGCTGGAGACTCTGCTGCAGTTCACTATAACCCAACCCACCAGAACGCT TACATCCCACTGGCTACCAATGCTGTCCGTCAGGGTATCCTAGTTGGAAAGAATCTGGTGAAACCTACCGTTA AGTACATGGGAACCCAGAGCAGCTCTGGATTGGCACTGTATGATCGTACTATCGTTTCCACCGGACTGACTCT GGCAGCTGCTAAGCAGCAAGGTCTTAATGCTGAGCAGGTTATCGTGGAAGATAACTATCGCCCGGAGTTTATG CCCTCTACTGAACCTGTCCTGATGTCTCTGGTTTTTGACCCCGACACCCATCGTATCCTGGGAGGAGCACTGA TGTCTAAATACGATGTCTCTCAATCAGCAAACACTCTTAGCGTCTGCATCCAGAACGAGAACACCATTGACGA CCTTGCAATGGTAGACATGCTGTTCCAGCCAAACTTTGACCGTCCTTTCAACTACCTTAACATCTTGGCCCAG GCTGCTCAGGCCAAGGTGGCACAGTCTGTGAACGCTTGA SEQ ID NO: 15 - The amino acid sequence of Lactobacillus brevis NAD(P)H oxidase MKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQGLFYSSPEELQKLGANV QMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKLCKNWAHAQALIEDAKE AKRITVIGAGYIGAELAEAYSTTGHDVTLIDAMARVMPKYFDADFTDVIEQDYRDHGVQLALGETVESFTDSA TGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFAAGDSAAVHYNPTHQNA YIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGLNAEQVIVEDNYRPEFM PSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLFQPNFDRPFNYLNILAQ AAQAKVAQSVNA SEQ ID NO: 16 - The codon optimised nucleotide sequence of Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R ATGAAAGTCACCGTGGTGGGATGCACCCACGCAGGTACCTTCGCTATTAAGCAGATCCTGGCTGAGCACCCCG ATGCAGAAGTCACCGTTTATGAACGTAATGACGTGATCAGCTTCCTGTCTTGCGGTATTGCCCTGTACCTTGG AGGGAAGGTTGCCGACCCTCAGGGACTGTTCTATTCTTCTCCCGAAGAGCTGCAGAAACTGGGTGCAAATGTT CAGATGAACCACAATGTTCTGGCAATTGACCCCGACCAGAAAACTGTTACCGTAGAGGACCTCACTAATCATG CTCAGACTACCGAGTCGTACGACAAGCTGGTGATGACCTCTGGTTCTTGGCCTATCGTCCCCAAGATTCCAGG TATCGACAGCGACCGCGTGAAGTTGTGCAAAAACTGGGCTCACGCTCAAGCACTGATTGAGGACGCTAAGGAA GCAAAACGCATCACTGTTATCGGAGCTGGTTATATTGCTGCGGAGCTGGCAGAAGCGTATTCTACTACTGGAC ACGACGTTACCCTGATCGCACGTAGCGCACGCGTTATGCGTAAGTACTTCGATGCTGATTTCACTGACGTGAT CGAACAGGATTATCGTGACCACGGTGTCCAGCTTGCTCTGGGAGAGACTGTGGAGTCCTTCACCGACTCTGCT ACCGGACTGACTATCAAAACTGACAAGAACTCCTACGAGACTGATCTGGCTATCCTGTGCATAGGTTTTCGTC CCAACACCGACCTGCTTAAGGGTAAGGTTGACATGGCACCTAACGGAGCTATCATCACTGATGACTACATGCG TTCCTCTAACCCCGATATTTTCGCCGCCGGTGATTCTGCCGCAGTTCATTATAACCCCACTCACCAGAACGCA TACATCCCACTGGCCACCAACGCTGTCCGTCAGGGCATCCTGGTCGGAAAGAACTTGGTCAAGCCAACGGTCA AATATATGGGAACACAAAGCTCTTCTGGTCTTGCACTTTACGATCGTACCATTGTTTCTACCGGACTGACCCT GGCTGCAGCTAAGCAGCAGGGTCTGAATGCAGAGCAGGTCATTGTCGAGGACAATTACCGTCCTGAGTTTATG CCCAGCACTGAGCCAGTCTTGATGAGCCTTGTGTTCGATCCGGACACTCACCGCATCCTGGGAGGTGCACTGA TGTCAAAGTACGACGTTTCTCAATCTGCTAACACTCTGTCTGTTTGTATTCAGAACGAGAATACTATTGACGA CCTGGCTATGGTGGACATGCTGTTTCAGCCCAACTTTGATCGCCCCTTCAACTACCTGAATATCCTGGCTCAG GCCGCACAGGCAAAGGTTGCACAATCGGTTAACGCATGA SEQ ID NO: 17 - The amino acid sequence of Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R MKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQGLFYSSPEELQKLGANV QMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKLCKNWAHAQALIEDAKE AKRITVIGAGYIAAELAEAYSTTGHDVTLIARSARVMRKYFDADFTDVIEQDYRDHGVQLALGETVESFTDSA TGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFAAGDSAAVHYNPTHQNA YIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGLNAEQVIVEDNYRPEFM PSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLFQPNFDRPFNYLNILAQ AAQAKVAQSVNA SEQ ID NO: 18 - The codon optimised nucleotide sequence of Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R ATGAGCAAGATTGTTATCGTTGGAGCCAATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATG GATCTGAGAATGAGGTGGTTGTCTTTGACCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTG GATCGGTAAGCAGATCTCTGGTCCCCAGGGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCC AAGATTTACATGGAGAGCCCTGTCACTGCTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGAC AGGAGCACGTCGAATCTTACGAGAAGCTGATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGG TGCAGCAATCAAGGAGGGTAGCCGTGATTTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAG AACGCTGAGGACGTTATTAACAAACTGCAGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAG GTTACATTGGTGTCGAACTGGCAGAAGCATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGA CACCTGTTTGCGTGGTTACTACGATCAAGATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATA GAGCTTGCATTTGGAGAAACTGTTAAAGCAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAG CATCTCATGACGTCGACATGGTGATCCTGGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCT GAAAACTTTCCGTAACGGAGCCTTCCTTGTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATT GGTGATTGCGCTACCGTGTACGACAACGCAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTC GTTCTGGTATTGTAGCCGGACACAACGCTGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGG TATCTCTATTTTCGGACTGAACATGGTTTCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAAT CCTGAAGTCACCGCATTCACTGATTTCCAGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGA AGATCGTGTACGACAAAGACTCTCGTCTGGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGG TATCCATATGTTTAGCCTTGCCATTCAGGAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTT CTTCCCCACTTTAACCAGCCTTACAATTATATGATCAAGGCCGCTCTGAAAGCAAAGTGA SEQ ID NO: 19 - The amino acid sequence of Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R MSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQGLFYADKESLEAKGA KIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRDFEATLKNLQFVKLYQ NAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQDLSEMMRQNLEDHGI ELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFLVDKKQETSIPDVYAI GDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMVSTGLTQEKAKRFGYN PEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQEKVTIERLALLDYFF LPHFNQPYNYMIKAALKAK SEQ ID NO: 20 - The codon optimised nucleotide sequence of Arabidopsis thaliana rubisco small subunit fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R ATGGCTTCTTCTATGCTGTCCAGCGCTACTATGGTGGCATCTCCCGCACAGGCTACCATGGTCGCTCCCTTCA ATGGCTTGAAATCTTCCGCTGCCTTCCCCGCAACACGCAAGGCGAACAATGATATCACTAGCATTACCTCTAA CGGAGGTCGTGTCAATTGTATGCAGGTGTGGCCTCCCATCGGTAAAAAGAAGTTCGAAACCCTGAGCTACCTG CCTGACCTGACTGACTCTGAGCTGGCAAAGGAGGTTGACTATCTGATCCGTAACAAGTGGATTCCCTGCGTTG AGTTTGAGCTCGAGCATGGGTTCGTTTACCGTGAGCACGGAAACTCTCCCGGATATTACGACGGTCGTTACTG GACCATGTGGAAACTGCCACTTTTCGGTTGCACTGATTCTGCACAGGTCCTTAAGGAAGTTGAGGAATGCAAA AAGGAGTATCCAAACGCATTCATCCGTATCATTGGATTTGACAACACTCGCCAGGTGCAATGCATTTCATTCA TCGCCTACAAGCCCCCTTCGTTTACCGGTGGATCTGGTggaggtATGAGCAAGATTGTTATCGTTGGAGCCAA TCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGAC CAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAGG GACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTGC TATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCTG ATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGATT TCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGCA GGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGCA TTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAAG ATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAGC AATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCTG GCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTTG TGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACGC AATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGCT GCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTTT CTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCCA GAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCTG GTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAGG AGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATTA TATGATCAAGGCCGCTCTGAAAGCAAAGTGA SEQ ID NO: 21 - The amino acid sequence of Arabidopsis thaliana rubisco small subunit fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R MASSMLSSATMVASPAQATMVAPFNGLKSSAAFPATRKANNDITSITSNGGRVNCMQVWPPIGKKKFETLSYL PDLTDSELAKEVDYLIRNKWIPCVEFELEHGFVYREHGNSPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECK KEYPNAFIRIIGFDNTRQVQCISFIAYKPPSFTGGSGGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFD QNSNISFLGCGMALWIGKQISGPQGLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKL ILATGSTPILPPIKGAAIKEGSRDFEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEA FKRLGKEVILIARHDTCLRGYYDQDLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVIL AVGFRPNTALGNAKLKTFRNGAFLVDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNA AGHKLESLGVQGSNGISIFGLNMVSTGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRL VLGAQMASKEDMSMGIHMFSLAIQEKVTIERLALLDYFFLPHFNQPYNYMIKAALKAK SEQ ID NO: 22 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R ATGGCTTCTATGGGCGGACTGCACGGGGCCTCCCCCGCAGTCTTGGAGGGAAGCCTGAAGATCAACGGTTCTT CACGTCTGAATGGATCTGGACGCGTGGCTGTTGCACAGCGCTCTCGTCTGGTTGTGCGTGCTCAGCAGTCGGA GGAAACCTCTCGTCGTAGCGTCATTGGTCTTGTCGCAGCGGGTCTGGCAGGTGGTTCTTTCGTTCAAGCTGTG CTGGCTGACGCAATCAGCATTAAAGTTGGACCCCCTCCCGCCGGAGGTATGAGCAAGATTGTTATCGTTGGAG CCAATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTT TGACCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCC CAGGGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCA CTGCTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAA GCTGATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGT GATTTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAAC TGCAGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGA AGCATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGAT CAAGATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTA AAGCAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGAT CCTGGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTC CTTGTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACA ACGCAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAA CGCTGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATG GTTTCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATT TCCAGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCG TCTGGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATT CAGGAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACA ATTATATGATCAAGGCCGCTCTGAAAGCAAAGTGA SEQ ID NO: 23 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R MASMGGLHGASPAVLEGSLKINGSSRLNGSGRVAVAQRSRLVVRAQQSEETSRRSVIGLVAAGLAGGSFVQAV LADAISIKVGPPPAGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGP QGLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSR DFEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYD QDLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAF LVDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNM VSTGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAI QEKVTIERLALLDYFFLPHFNQPYNYMIKAALKAK SEQ ID NO: 24 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R ATGGCCTACAGCGCTTGTTTCCTGCACCAGAGCGCTCTGGCTTCTTCTGCTGCACGTTCTTCCTCCTCATCTT CTTCCCAGCGTCACGTGTCTCTTTCTAAGCCCGTCCAGATTATCTGCAAAGCACAACAGAGCCATGAGGACGA TAACTCTGCAGTTTCTCGTCGCCTGGCATTGACCCTGCTGGTTGGAGCGGCAGCTGTCGGTTCAAAGGTTAGC CCTGCAGACGCCGGAGGTATGAGCAAGATTGTTATCGTTGGAGCCAATCACGCAGGAACCGCTGCAATCAACA CTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGACCAGAACTCAAACATTAGCTTCCTGGG ATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAGGGACTGTTCTATGCAGACAAGGAGTCT CTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTGCTATCGACTACGATGCTAAACGCGTGA CCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCTGATCCTGGCCACTGGATCCACTCCCAT TCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGATTTCGAGGCGACCTTGAAGAACCTGCAA TTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGCAGGACAAGACCCAAAATCTGAACCGTA TTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGCATTCAAGCGCCTGGGTAAGGAAGTTAT TCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAAGATCTATCCGAGATGATGCGTCAGAAC TTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAGCAATCGAGGGTGACGGAAAAGTGGAGC GCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCTGGCTGTCGGATTCCGCCCCAATACCGC TCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTTGTGGATAAGAAACAGGAGACTAGCATT CCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACGCAATCAATGACACTAACTACATCGCGC TGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGCTGCTGGACACAAGCTGGAGTCTTTGGG AGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTTTCTACCGGTCTGACTCAGGAAAAGGCT AAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCCAGAAGGCATCTTTCATCGAGCACGACA ACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCTGGTTCTCGGAGCTCAGATGGCTTCTAA GGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAGGAGAAGGTTACCATCGAACGTCTGGCA CTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATTATATGATCAAGGCCGCTCTGAAAGCAA AGTGA SEQ ID NO: 25 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVS PADAGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQGLFYADKES LEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRDFEATLKNLQ FVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQDLSEMMRQN LEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFLVDKKQETSI PDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMVSTGLTQEKA KRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQEKVTIERLA LLDYFFLPHFNQPYNYMIKAALKAK SEQ ID NO: 26 - The codon optimised nucleotide sequence of Arabidopsis thaliana outer envelope protein 9 fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R ATGGGTAACGAAACCAAGACTAATGGGGGTCCTGCTAGCATGGCTGGAGGCGGAGGTTTCCGTGCAAAAATGG AGCATTACGTTTACTCTGGTGAAAAGAAGCACGTCCTTGTCGGTATCGGAATCGTTACCATTATTTTTGGAGT GCCCTGGTATCTGATGACTCAGGGATCTAAACACCAGAGCCACCAAGACTATATGGATAAGGCCGACAAGGCA CGCAAGGCTCGTCTGTCCTCTTCATCTTCTGCAAACAAAGGAGGTATGAGCAAGATTGTTATCGTTGGAGCCA ATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGA CCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAG GGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTG CTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCT GATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGAT TTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGC AGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGC ATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAA GATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAG CAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCT GGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTT GTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACG CAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGC TGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTT TCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCC AGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCT GGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAG GAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATT ATATGATCAAGGCCGCTCTGAAAGCAAAGTGA SEQ ID NO: 27 - The amino acid sequence of Arabidopsis thaliana outer envelope protein 9 fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R MGNETKTNGGPASMAGGGGFRAKMEHYVYSGEKKHVLVGIGIVTIIFGVPWYLMTQGSKHQSHQDYMDKADKA RKARLSSSSSANKGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQ GLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRD FEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQ DLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFL VDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMV STGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQ EKVTIERLALLDYFFLPHFNQPYNYMIKAALKAK SEQ ID NO: 28 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R ATGGCTTCTATGGGCGGACTGCACGGGGCCTCCCCCGCAGTCTTGGAGGGAAGCCTGAAGATCAACGGTTCTT CACGTCTGAATGGATCTGGACGCGTGGCTGTTGCACAGCGCTCTCGTCTGGTTGTGCGTGCTCAGCAGTCGGA GGAAACCTCTCGTCGTAGCGTCATTGGTCTTGTCGCAGCGGGTCTGGCAGGTGGTTCTTTCGTTCAAGCTGTG CTGGCTGACGCAATCAGCATTAAAGTTGGACCCCCTCCCGCCGGAGGTATGAAAGTCACCGTGGTGGGATGCA CCCACGCAGGTACCTTCGCTATTAAGCAGATCCTGGCTGAGCACCCCGATGCAGAAGTCACCGTTTATGAACG TAATGACGTGATCAGCTTCCTGTCTTGCGGTATTGCCCTGTACCTTGGAGGGAAGGTTGCCGACCCTCAGGGA CTGTTCTATTCTTCTCCCGAAGAGCTGCAGAAACTGGGTGCAAATGTTCAGATGAACCACAATGTTCTGGCAA TTGACCCCGACCAGAAAACTGTTACCGTAGAGGACCTCACTAATCATGCTCAGACTACCGAGTCGTACGACAA GCTGGTGATGACCTCTGGTTCTTGGCCTATCGTCCCCAAGATTCCAGGTATCGACAGCGACCGCGTGAAGTTG TGCAAAAACTGGGCTCACGCTCAAGCACTGATTGAGGACGCTAAGGAAGCAAAACGCATCACTGTTATCGGAG CTGGTTATATTGCTGCGGAGCTGGCAGAAGCGTATTCTACTACTGGACACGACGTTACCCTGATCGCACGTAG CGCACGCGTTATGCGTAAGTACTTCGATGCTGATTTCACTGACGTGATCGAACAGGATTATCGTGACCACGGT GTCCAGCTTGCTCTGGGAGAGACTGTGGAGTCCTTCACCGACTCTGCTACCGGACTGACTATCAAAACTGACA AGAACTCCTACGAGACTGATCTGGCTATCCTGTGCATAGGTTTTCGTCCCAACACCGACCTGCTTAAGGGTAA GGTTGACATGGCACCTAACGGAGCTATCATCACTGATGACTACATGCGTTCCTCTAACCCCGATATTTTCGCC GCCGGTGATTCTGCCGCAGTTCATTATAACCCCACTCACCAGAACGCATACATCCCACTGGCCACCAACGCTG TCCGTCAGGGCATCCTGGTCGGAAAGAACTTGGTCAAGCCAACGGTCAAATATATGGGAACACAAAGCTCTTC TGGTCTTGCACTTTACGATCGTACCATTGTTTCTACCGGACTGACCCTGGCTGCAGCTAAGCAGCAGGGTCTG AATGCAGAGCAGGTCATTGTCGAGGACAATTACCGTCCTGAGTTTATGCCCAGCACTGAGCCAGTCTTGATGA GCCTTGTGTTCGATCCGGACACTCACCGCATCCTGGGAGGTGCACTGATGTCAAAGTACGACGTTTCTCAATC TGCTAACACTCTGTCTGTTTGTATTCAGAACGAGAATACTATTGACGACCTGGCTATGGTGGACATGCTGTTT CAGCCCAACTTTGATCGCCCCTTCAACTACCTGAATATCCTGGCTCAGGCCGCACAGGCAAAGGTTGCACAAT CGGTTAACGCATGA SEQ ID NO: 29 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R MASMGGLHGASPAVLEGSLKINGSSRLNGSGRVAVAQRSRLVVRAQQSEETSRRSVIGLVAAGLAGGSFVQAV LADAISIKVGPPPAGGMKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQG LFYSSPEELQKLGANVQMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKL CKNWAHAQALIEDAKEAKRITVIGAGYIAAELAEAYSTTGHDVTLIARSARVMRKYFDADFTDVIEQDYRDHG VQLALGETVESFTDSATGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFA AGDSAAVHYNPTHQNAYIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGL NAEQVIVEDNYRPEFMPSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLF QPNFDRPFNYLNILAQAAQAKVAQSVNA SEQ ID NO: 30 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R ATGGCCTACAGCGCTTGTTTCCTGCACCAGAGCGCTCTGGCTTCTTCTGCTGCACGTTCTTCCTCCTCATCTT CTTCCCAGCGTCACGTGTCTCTTTCTAAGCCCGTCCAGATTATCTGCAAAGCACAACAGAGCCATGAGGACGA TAACTCTGCAGTTTCTCGTCGCCTGGCATTGACCCTGCTGGTTGGAGCGGCAGCTGTCGGTTCAAAGGTTAGC CCTGCAGACGCCggaggtATGAAAGTCACCGTGGTGGGATGCACCCACGCAGGTACCTTCGCTATTAAGCAGA TCCTGGCTGAGCACCCCGATGCAGAAGTCACCGTTTATGAACGTAATGACGTGATCAGCTTCCTGTCTTGCGG TATTGCCCTGTACCTTGGAGGGAAGGTTGCCGACCCTCAGGGACTGTTCTATTCTTCTCCCGAAGAGCTGCAG AAACTGGGTGCAAATGTTCAGATGAACCACAATGTTCTGGCAATTGACCCCGACCAGAAAACTGTTACCGTAG AGGACCTCACTAATCATGCTCAGACTACCGAGTCGTACGACAAGCTGGTGATGACCTCTGGTTCTTGGCCTAT CGTCCCCAAGATTCCAGGTATCGACAGCGACCGCGTGAAGTTGTGCAAAAACTGGGCTCACGCTCAAGCACTG ATTGAGGACGCTAAGGAAGCAAAACGCATCACTGTTATCGGAGCTGGTTATATTGCTGCGGAGCTGGCAGAAG CGTATTCTACTACTGGACACGACGTTACCCTGATCGCACGTAGCGCACGCGTTATGCGTAAGTACTTCGATGC TGATTTCACTGACGTGATCGAACAGGATTATCGTGACCACGGTGTCCAGCTTGCTCTGGGAGAGACTGTGGAG TCCTTCACCGACTCTGCTACCGGACTGACTATCAAAACTGACAAGAACTCCTACGAGACTGATCTGGCTATCC TGTGCATAGGTTTTCGTCCCAACACCGACCTGCTTAAGGGTAAGGTTGACATGGCACCTAACGGAGCTATCAT CACTGATGACTACATGCGTTCCTCTAACCCCGATATTTTCGCCGCCGGTGATTCTGCCGCAGTTCATTATAAC CCCACTCACCAGAACGCATACATCCCACTGGCCACCAACGCTGTCCGTCAGGGCATCCTGGTCGGAAAGAACT TGGTCAAGCCAACGGTCAAATATATGGGAACACAAAGCTCTTCTGGTCTTGCACTTTACGATCGTACCATTGT TTCTACCGGACTGACCCTGGCTGCAGCTAAGCAGCAGGGTCTGAATGCAGAGCAGGTCATTGTCGAGGACAAT TACCGTCCTGAGTTTATGCCCAGCACTGAGCCAGTCTTGATGAGCCTTGTGTTCGATCCGGACACTCACCGCA TCCTGGGAGGTGCACTGATGTCAAAGTACGACGTTTCTCAATCTGCTAACACTCTGTCTGTTTGTATTCAGAA CGAGAATACTATTGACGACCTGGCTATGGTGGACATGCTGTTTCAGCCCAACTTTGATCGCCCCTTCAACTAC CTGAATATCCTGGCTCAGGCCGCACAGGCAAAGGTTGCACAATCGGTTAACGCATGA SEQ ID NO: 31 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVS PADAGGMKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQGLFYSSPEELQ KLGANVQMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKLCKNWAHAQAL IEDAKEAKRITVIGAGYIAAELAEAYSTTGHDVTLIARSARVMRKYFDADFTDVIEQDYRDHGVQLALGETVE SFTDSATGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFAAGDSAAVHYN PTHQNAYIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGLNAEQVIVEDN YRPEFMPSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLFQPNFDRPFNY LNILAQAAQAKVAQSVNA SEQ ID NO: 32 - The codon optimised nucleotide sequence of Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP ATGAGCAAGATTGTTATCGTTGGAGCCAATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATG GATCTGAGAATGAGGTGGTTGTCTTTGACCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTG GATCGGTAAGCAGATCTCTGGTCCCCAGGGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCC AAGATTTACATGGAGAGCCCTGTCACTGCTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGAC AGGAGCACGTCGAATCTTACGAGAAGCTGATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGG TGCAGCAATCAAGGAGGGTAGCCGTGATTTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAG AACGCTGAGGACGTTATTAACAAACTGCAGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAG GTTACATTGGTGTCGAACTGGCAGAAGCATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGA CACCTGTTTGCGTGGTTACTACGATCAAGATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATA GAGCTTGCATTTGGAGAAACTGTTAAAGCAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAG CATCTCATGACGTCGACATGGTGATCCTGGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCT GAAAACTTTCCGTAACGGAGCCTTCCTTGTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATT GGTGATTGCGCTACCGTGTACGACAACGCAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTC GTTCTGGTATTGTAGCCGGACACAACGCTGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGG TATCTCTATTTTCGGACTGAACATGGTTTCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAAT CCTGAAGTCACCGCATTCACTGATTTCCAGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGA AGATCGTGTACGACAAAGACTCTCGTCTGGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGG TATCCATATGTTTAGCCTTGCCATTCAGGAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTT CTTCCCCACTTTAACCAGCCTTACAATTATATGATCAAGGCCGCTCTGAAAGCAAAGGGTGGTTCGGCTGTGA GCAAGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAA GTTCAGCGTGTCCGGCGAGGGCGAGGGCGATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACC GGCAAGCTGCCCGTGCCCTGGCCCACCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACC CCGACCACATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTT CTTCAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATC GAGCTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCC ACAACGTCTATATCATGGCCGACAAGCAGAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGA GGACGGCAGCGTGCAGCTCGCCGACCACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCC GACAACCACTACCTGAGTACTCAGTCCAAGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGC TGGAGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 33 - The amino acid sequence of Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP MSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQGLFYADKESLEAKGA KIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRDFEATLKNLQFVKLYQ NAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQDLSEMMRQNLEDHGI ELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFLVDKKQETSIPDVYAI GDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMVSTGLTQEKAKRFGYN PEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQEKVTIERLALLDYFF LPHFNQPYNYMIKAALKAKGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTT GKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRI ELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLP DNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 34 - The codon optimised nucleotide sequence of Arabidopsis thaliana rubisco small subunit fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP ATGGCTTCTTCTATGCTGTCCAGCGCTACTATGGTGGCATCTCCCGCACAGGCTACCATGGTCGCTCCCTTCA ATGGCTTGAAATCTTCCGCTGCCTTCCCCGCAACACGCAAGGCGAACAATGATATCACTAGCATTACCTCTAA CGGAGGTCGTGTCAATTGTATGCAGGTGTGGCCTCCCATCGGTAAAAAGAAGTTCGAAACCCTGAGCTACCTG CCTGACCTGACTGACTCTGAGCTGGCAAAGGAGGTTGACTATCTGATCCGTAACAAGTGGATTCCCTGCGTTG AGTTTGAGCTCGAGCATGGGTTCGTTTACCGTGAGCACGGAAACTCTCCCGGATATTACGACGGTCGTTACTG GACCATGTGGAAACTGCCACTTTTCGGTTGCACTGATTCTGCACAGGTCCTTAAGGAAGTTGAGGAATGCAAA AAGGAGTATCCAAACGCATTCATCCGTATCATTGGATTTGACAACACTCGCCAGGTGCAATGCATTTCATTCA TCGCCTACAAGCCCCCTTCGTTTACCGGTGGATCTGGTGGAGGTATGAGCAAGATTGTTATCGTTGGAGCCAA TCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGAC CAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAGG GACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTGC TATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCTG ATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGATT TCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGCA GGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGCA TTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAAG ATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAGC AATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCTG GCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTTG TGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACGC AATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGCT GCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTTT CTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCCA GAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCTG GTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAGG AGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATTA TATGATCAAGGCCGCTCTGAAAGCAAAGGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGTG GTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGCG ATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGGCCCACCCT CGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACGACTTCTTC AAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTACAAGACCC GCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGGA CGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAAGCAG AAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGCCGACCACT ACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACTCAGTCCAA GCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCACT CTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 35 - The amino acid sequence of Arabidopsis thaliana rubisco small subunit fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP MASSMLSSATMVASPAQATMVAPFNGLKSSAAFPATRKANNDITSITSNGGRVNCMQVWPPIGKKKFETLSYL PDLTDSELAKEVDYLIRNKWIPCVEFELEHGFVYREHGNSPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECK KEYPNAFIRIIGFDNTRQVQCISFIAYKPPSFTGGSGGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFD QNSNISFLGCGMALWIGKQISGPQGLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKL ILATGSTPILPPIKGAAIKEGSRDFEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEA FKRLGKEVILIARHDTCLRGYYDQDLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVIL AVGFRPNTALGNAKLKTFRNGAFLVDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNA AGHKLESLGVQGSNGISIFGLNMVSTGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRL VLGAQMASKEDMSMGIHMFSLAIQEKVTIERLALLDYFFLPHFNQPYNYMIKAALKAKGGSAVSKGEELFTGV VPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFF KSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQ KNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGIT LGMDELYK SEQ ID NO: 36 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP ATGGCTTCTATGGGCGGACTGCACGGGGCCTCCCCCGCAGTCTTGGAGGGAAGCCTGAAGATCAACGGTTCTT CACGTCTGAATGGATCTGGACGCGTGGCTGTTGCACAGCGCTCTCGTCTGGTTGTGCGTGCTCAGCAGTCGGA GGAAACCTCTCGTCGTAGCGTCATTGGTCTTGTCGCAGCGGGTCTGGCAGGTGGTTCTTTCGTTCAAGCTGTG CTGGCTGACGCAATCAGCATTAAAGTTGGACCCCCTCCCGCCGGAGGTATGAGCAAGATTGTTATCGTTGGAG CCAATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTT TGACCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCC CAGGGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCA CTGCTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAA GCTGATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGT GATTTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAAC TGCAGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGA AGCATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGAT CAAGATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTA AAGCAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGAT CCTGGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTC CTTGTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACA ACGCAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAA CGCTGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATG GTTTCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATT TCCAGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCG TCTGGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATT CAGGAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACA ATTATATGATCAAGGCCGCTCTGAAAGCAAAGGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCACCGG GGTGGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAG GGCGATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGGCCCA CCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACGACTT CTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTACAAG ACCCGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGG AGGACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAA GCAGAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGCCGAC CACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACTCAGT CCAAGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGAT CACTCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 37 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP MASMGGLHGASPAVLEGSLKINGSSRLNGSGRVAVAQRSRLVVRAQQSEETSRRSVIGLVAAGLAGGSFVQAV LADAISIKVGPPPAGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGP QGLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSR DFEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYD QDLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAF LVDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNM VSTGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAI QEKVTIERLALLDYFFLPHFNQPYNYMIKAALKAKGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGE GDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYK TRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLAD HYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 38 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP ATGGCCTACAGCGCTTGTTTCCTGCACCAGAGCGCTCTGGCTTCTTCTGCTGCACGTTCTTCCTCCTCATCTT CTTCCCAGCGTCACGTGTCTCTTTCTAAGCCCGTCCAGATTATCTGCAAAGCACAACAGAGCCATGAGGACGA TAACTCTGCAGTTTCTCGTCGCCTGGCATTGACCCTGCTGGTTGGAGCGGCAGCTGTCGGTTCAAAGGTTAGC CCTGCAGACGCCGGAGGTATGAGCAAGATTGTTATCGTTGGAGCCAATCACGCAGGAACCGCTGCAATCAACA CTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGACCAGAACTCAAACATTAGCTTCCTGGG ATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAGGGACTGTTCTATGCAGACAAGGAGTCT CTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTGCTATCGACTACGATGCTAAACGCGTGA CCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCTGATCCTGGCCACTGGATCCACTCCCAT TCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGATTTCGAGGCGACCTTGAAGAACCTGCAA TTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGCAGGACAAGACCCAAAATCTGAACCGTA TTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGCATTCAAGCGCCTGGGTAAGGAAGTTAT TCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAAGATCTATCCGAGATGATGCGTCAGAAC TTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAGCAATCGAGGGTGACGGAAAAGTGGAGC GCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCTGGCTGTCGGATTCCGCCCCAATACCGC TCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTTGTGGATAAGAAACAGGAGACTAGCATT CCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACGCAATCAATGACACTAACTACATCGCGC TGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGCTGCTGGACACAAGCTGGAGTCTTTGGG AGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTTTCTACCGGTCTGACTCAGGAAAAGGCT AAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCCAGAAGGCATCTTTCATCGAGCACGACA ACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCTGGTTCTCGGAGCTCAGATGGCTTCTAA GGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAGGAGAAGGTTACCATCGAACGTCTGGCA CTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATTATATGATCAAGGCCGCTCTGAAAGCAA AGGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGAGCTGGACGG CGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGCGATGCCACCTACGGCAAGCTGACCCTG AAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGGCCCACCCTCGTGACCACCCTGACCTACGGCGTGC AGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGT CCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGAC ACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTGGGGCACAAGCTGG AGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAAGCAGAAGAACGGCATCAAGGTGAACTTCAA GATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGCCGACCACTACCAGCAGAACACCCCCATCGGCGAC GGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACTCAGTCCAAGCTGAGCAAAGACCCCAACGAGAAGC GCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCTGTACAAATG A SEQ ID NO: 39 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVS PADAGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQGLFYADKES LEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRDFEATLKNLQ FVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQDLSEMMRQN LEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFLVDKKQETSI PDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMVSTGLTQEKA KRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQEKVTIERLA LLDYFFLPHFNQPYNYMIKAALKAKGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTL KFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGD TLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGD GPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 40 - The codon optimised nucleotide sequence of Arabidopsis thaliana outer envelope protein 9 fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP ATGGGTAACGAAACCAAGACTAATGGGGGTCCTGCTAGCATGGCTGGAGGCGGAGGTTTCCGTGCAAAAATGG AGCATTACGTTTACTCTGGTGAAAAGAAGCACGTCCTTGTCGGTATCGGAATCGTTACCATTATTTTTGGAGT GCCCTGGTATCTGATGACTCAGGGATCTAAACACCAGAGCCACCAAGACTATATGGATAAGGCCGACAAGGCA CGCAAGGCTCGTCTGTCCTCTTCATCTTCTGCAAACAAAGGAGGTATGAGCAAGATTGTTATCGTTGGAGCCA ATCACGCAGGAACCGCTGCAATCAACACTGTGCTGGACAACTATGGATCTGAGAATGAGGTGGTTGTCTTTGA CCAGAACTCAAACATTAGCTTCCTGGGATGCGGAATGGCTCTGTGGATCGGTAAGCAGATCTCTGGTCCCCAG GGACTGTTCTATGCAGACAAGGAGTCTCTGGAGGCTAAAGGTGCCAAGATTTACATGGAGAGCCCTGTCACTG CTATCGACTACGATGCTAAACGCGTGACCGCACTGGTCAACGGACAGGAGCACGTCGAATCTTACGAGAAGCT GATCCTGGCCACTGGATCCACTCCCATTCTGCCACCCATCAAGGGTGCAGCAATCAAGGAGGGTAGCCGTGAT TTCGAGGCGACCTTGAAGAACCTGCAATTCGTTAAGCTGTATCAGAACGCTGAGGACGTTATTAACAAACTGC AGGACAAGACCCAAAATCTGAACCGTATTGCTGTTGTTGGTGCAGGTTACATTGGTGTCGAACTGGCAGAAGC ATTCAAGCGCCTGGGTAAGGAAGTTATTCTGATTGCACGTCACGACACCTGTTTGCGTGGTTACTACGATCAA GATCTATCCGAGATGATGCGTCAGAACTTGGAGGACCACGGCATAGAGCTTGCATTTGGAGAAACTGTTAAAG CAATCGAGGGTGACGGAAAAGTGGAGCGCATCGTCACTGATAAAGCATCTCATGACGTCGACATGGTGATCCT GGCTGTCGGATTCCGCCCCAATACCGCTCTGGGCAACGCTAAGCTGAAAACTTTCCGTAACGGAGCCTTCCTT GTGGATAAGAAACAGGAGACTAGCATTCCAGACGTGTATGCTATTGGTGATTGCGCTACCGTGTACGACAACG CAATCAATGACACTAACTACATCGCGCTGGCATCCAATGCTCTTCGTTCTGGTATTGTAGCCGGACACAACGC TGCTGGACACAAGCTGGAGTCTTTGGGAGTCCAGGGTTCGAATGGTATCTCTATTTTCGGACTGAACATGGTT TCTACCGGTCTGACTCAGGAAAAGGCTAAGCGCTTTGGGTACAATCCTGAAGTCACCGCATTCACTGATTTCC AGAAGGCATCTTTCATCGAGCACGACAACTATCCCGTTACACTGAAGATCGTGTACGACAAAGACTCTCGTCT GGTTCTCGGAGCTCAGATGGCTTCTAAGGAGGATATGTCTATGGGTATCCATATGTTTAGCCTTGCCATTCAG GAGAAGGTTACCATCGAACGTCTGGCACTGCTGGACTATTTCTTTCTTCCCCACTTTAACCAGCCTTACAATT ATATGATCAAGGCCGCTCTGAAAGCAAAGGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGT GGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGC GATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGGCCCACCC TCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACGACTTCTT CAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTACAAGACC CGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGG ACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAAGCA GAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGCCGACCAC TACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACTCAGTCCA AGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCAC TCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 41 - The amino acid sequence of Arabidopsis thaliana outer envelope protein 9 fused to Streptococcus mutans NAD(P)H oxidase, containing mutations 192A / 193R / 194H / 199R, fused to monomeric enhanced GFP MGNETKTNGGPASMAGGGGFRAKMEHYVYSGEKKHVLVGIGIVTIIFGVPWYLMTQGSKHQSHQDYMDKADKA RKARLSSSSSANKGGMSKIVIVGANHAGTAAINTVLDNYGSENEVVVFDQNSNISFLGCGMALWIGKQISGPQ GLFYADKESLEAKGAKIYMESPVTAIDYDAKRVTALVNGQEHVESYEKLILATGSTPILPPIKGAAIKEGSRD FEATLKNLQFVKLYQNAEDVINKLQDKTQNLNRIAVVGAGYIGVELAEAFKRLGKEVILIARHDTCLRGYYDQ DLSEMMRQNLEDHGIELAFGETVKAIEGDGKVERIVTDKASHDVDMVILAVGFRPNTALGNAKLKTFRNGAFL VDKKQETSIPDVYAIGDCATVYDNAINDTNYIALASNALRSGIVAGHNAAGHKLESLGVQGSNGISIFGLNMV STGLTQEKAKRFGYNPEVTAFTDFQKASFIEHDNYPVTLKIVYDKDSRLVLGAQMASKEDMSMGIHMFSLAIQ EKVTIERLALLDYFFLPHFNQPYNYMIKAALKAKGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEG DATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKT RAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADH YQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 42 - The codon optimised nucleotide sequence of Lactobacillus brevis NAD(P)H oxidase fused to monomeric enhanced GFP ATGAAGGTGACTGTCGTGGGCTGCACACACGCTGGTACGTTCGCAATTAAACAGATTCTGGCAGAGCACCCCG ATGCGGAGGTTACCGTTTACGAGCGTAATGATGTCATCTCGTTCCTGTCGTGTGGTATCGCACTGTACCTGGG TGGAAAGGTCGCAGACCCTCAGGGACTGTTCTACAGCTCTCCCGAGGAACTGCAGAAGCTGGGAGCAAACGTG CAGATGAACCACAACGTCCTGGCAATCGATCCCGACCAGAAAACTGTGACTGTTGAGGATCTGACCAACCACG CTCAAACCACTGAGTCTTACGATAAGCTGGTCATGACTTCTGGGTCCTGGCCTATTGTTCCAAAGATCCCCGG AATCGATAGCGACCGCGTGAAGCTGTGCAAGAATTGGGCGCACGCACAAGCCCTGATTGAGGACGCAAAGGAA GCAAAGCGTATTACTGTTATCGGTGCTGGTTATATCGGAGCAGAGCTCGCCGAGGCTTATTCTACCACTGGTC ATGACGTTACCCTTATTGACGCTATGGCTCGCGTTATGCCCAAGTATTTCGACGCTGACTTCACTGACGTCAT TGAACAGGACTACCGTGATCACGGTGTTCAGCTGGCACTGGGAGAGACTGTTGAATCTTTTACCGACTCTGCC ACCGGTTTGACCATTAAAACTGACAAGAATTCCTATGAGACTGATCTGGCCATTCTGTGCATTGGTTTCCGTC CCAACACTGACCTGCTTAAAGGTAAAGTTGACATGGCTCCCAATGGAGCAATAATCACCGACGACTACATGCG CTCTAGCAATCCCGACATCTTCGCCGCTGGAGACTCTGCTGCAGTTCACTATAACCCAACCCACCAGAACGCT TACATCCCACTGGCTACCAATGCTGTCCGTCAGGGTATCCTAGTTGGAAAGAATCTGGTGAAACCTACCGTTA AGTACATGGGAACCCAGAGCAGCTCTGGATTGGCACTGTATGATCGTACTATCGTTTCCACCGGACTGACTCT GGCAGCTGCTAAGCAGCAAGGTCTTAATGCTGAGCAGGTTATCGTGGAAGATAACTATCGCCCGGAGTTTATG CCCTCTACTGAACCTGTCCTGATGTCTCTGGTTTTTGACCCCGACACCCATCGTATCCTGGGAGGAGCACTGA TGTCTAAATACGATGTCTCTCAATCAGCAAACACTCTTAGCGTCTGCATCCAGAACGAGAACACCATTGACGA CCTTGCAATGGTAGACATGCTGTTCCAGCCAAACTTTGACCGTCCTTTCAACTACCTTAACATCTTGGCCCAG GCTGCTCAGGCCAAGGTGGCACAGTCTGTGAACGCTGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCA CCGGGGTGGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGG CGAGGGCGATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGG CCCACCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACG ACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTA CAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTC AAGGAGGACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCG ACAAGCAGAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGC CGACCACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACT CAGTCCAAGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCG GGATCACTCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 43 - The amino acid sequence of Lactobacillus brevis NAD(P)H oxidase fused to monomeric enhanced GFP MKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQGLFYSSPEELQKLGANV QMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKLCKNWAHAQALIEDAKE AKRITVIGAGYIGAELAEAYSTTGHDVTLIDAMARVMPKYFDADFTDVIEQDYRDHGVQLALGETVESFTDSA TGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFAAGDSAAVHYNPTHQNA YIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGLNAEQVIVEDNYRPEFM PSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLFQPNFDRPFNYLNILAQ AAQAKVAQSVNAGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPW PTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDF KEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLST QSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 44 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R, fused to monomeric enhanced GFP ATGGCTTCTATGGGCGGACTGCACGGGGCCTCCCCCGCAGTCTTGGAGGGAAGCCTGAAGATCAACGGTTCTT CACGTCTGAATGGATCTGGACGCGTGGCTGTTGCACAGCGCTCTCGTCTGGTTGTGCGTGCTCAGCAGTCGGA GGAAACCTCTCGTCGTAGCGTCATTGGTCTTGTCGCAGCGGGTCTGGCAGGTGGTTCTTTCGTTCAAGCTGTG CTGGCTGACGCAATCAGCATTAAAGTTGGACCCCCTCCCGCCGGAGGTATGAAAGTCACCGTGGTGGGATGCA CCCACGCAGGTACCTTCGCTATTAAGCAGATCCTGGCTGAGCACCCCGATGCAGAAGTCACCGTTTATGAACG TAATGACGTGATCAGCTTCCTGTCTTGCGGTATTGCCCTGTACCTTGGAGGGAAGGTTGCCGACCCTCAGGGA CTGTTCTATTCTTCTCCCGAAGAGCTGCAGAAACTGGGTGCAAATGTTCAGATGAACCACAATGTTCTGGCAA TTGACCCCGACCAGAAAACTGTTACCGTAGAGGACCTCACTAATCATGCTCAGACTACCGAGTCGTACGACAA GCTGGTGATGACCTCTGGTTCTTGGCCTATCGTCCCCAAGATTCCAGGTATCGACAGCGACCGCGTGAAGTTG TGCAAAAACTGGGCTCACGCTCAAGCACTGATTGAGGACGCTAAGGAAGCAAAACGCATCACTGTTATCGGAG CTGGTTATATTGCTGCGGAGCTGGCAGAAGCGTATTCTACTACTGGACACGACGTTACCCTGATCGCACGTAG CGCACGCGTTATGCGTAAGTACTTCGATGCTGATTTCACTGACGTGATCGAACAGGATTATCGTGACCACGGT GTCCAGCTTGCTCTGGGAGAGACTGTGGAGTCCTTCACCGACTCTGCTACCGGACTGACTATCAAAACTGACA AGAACTCCTACGAGACTGATCTGGCTATCCTGTGCATAGGTTTTCGTCCCAACACCGACCTGCTTAAGGGTAA GGTTGACATGGCACCTAACGGAGCTATCATCACTGATGACTACATGCGTTCCTCTAACCCCGATATTTTCGCC GCCGGTGATTCTGCCGCAGTTCATTATAACCCCACTCACCAGAACGCATACATCCCACTGGCCACCAACGCTG TCCGTCAGGGCATCCTGGTCGGAAAGAACTTGGTCAAGCCAACGGTCAAATATATGGGAACACAAAGCTCTTC TGGTCTTGCACTTTACGATCGTACCATTGTTTCTACCGGACTGACCCTGGCTGCAGCTAAGCAGCAGGGTCTG AATGCAGAGCAGGTCATTGTCGAGGACAATTACCGTCCTGAGTTTATGCCCAGCACTGAGCCAGTCTTGATGA GCCTTGTGTTCGATCCGGACACTCACCGCATCCTGGGAGGTGCACTGATGTCAAAGTACGACGTTTCTCAATC TGCTAACACTCTGTCTGTTTGTATTCAGAACGAGAATACTATTGACGACCTGGCTATGGTGGACATGCTGTTT CAGCCCAACTTTGATCGCCCCTTCAACTACCTGAATATCCTGGCTCAGGCCGCACAGGCAAAGGTTGCACAAT CGGTTAACGCAGGTGGTTCGGCTGTGAGCAAGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGA GCTGGACGGCGACGTAAACGGCCACAAGTTCAGCGTGTCCGGCGAGGGCGAGGGCGATGCCACCTACGGCAAG CTGACCCTGAAGTTCATCTGCACCACCGGCAAGCTGCCCGTGCCCTGGCCCACCCTCGTGACCACCCTGACCT ACGGCGTGCAGTGCTTCAGCCGCTACCCCGACCACATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGA AGGCTACGTCCAGGAGCGCACCATCTTCTTCAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTC GAGGGCGACACCCTGGTGAACCGCATCGAGCTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTGGGGC ACAAGCTGGAGTACAACTACAACAGCCACAACGTCTATATCATGGCCGACAAGCAGAAGAACGGCATCAAGGT GAACTTCAAGATCCGCCACAACATCGAGGACGGCAGCGTGCAGCTCGCCGACCACTACCAGCAGAACACCCCC ATCGGCGACGGCCCCGTGCTGCTGCCCGACAACCACTACCTGAGTACTCAGTCCAAGCTGAGCAAAGACCCCA ACGAGAAGCGCGATCACATGGTCCTGCTGGAGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCT GTACAAATGA SEQ ID NO: 45 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 16 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R, fused to monomeric enhanced GFP MASMGGLHGASPAVLEGSLKINGSSRLNGSGRVAVAQRSRLVVRAQQSEETSRRSVIGLVAAGLAGGSFVQAV LADAISIKVGPPPAGGMKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQG LFYSSPEELQKLGANVQMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKL CKNWAHAQALIEDAKEAKRITVIGAGYIAAELAEAYSTTGHDVTLIARSARVMRKYFDADFTDVIEQDYRDHG VQLALGETVESFTDSATGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFA AGDSAAVHYNPTHQNAYIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGL NAEQVIVEDNYRPEFMPSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLF QPNFDRPFNYLNILAQAAQAKVAQSVNAGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGK LTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKF EGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTP IGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK SEQ ID NO: 46 - The codon optimised nucleotide sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R, fused to monomeric enhanced GFP ATGGCCTACAGCGCTTGTTTCCTGCACCAGAGCGCTCTGGCTTCTTCTGCTGCACGTTCTTCCTCCTCATCTT CTTCCCAGCGTCACGTGTCTCTTTCTAAGCCCGTCCAGATTATCTGCAAAGCACAACAGAGCCATGAGGACGA TAACTCTGCAGTTTCTCGTCGCCTGGCATTGACCCTGCTGGTTGGAGCGGCAGCTGTCGGTTCAAAGGTTAGC CCTGCAGACGCCGGAGGTATGAAAGTCACCGTGGTGGGATGCACCCACGCAGGTACCTTCGCTATTAAGCAGA TCCTGGCTGAGCACCCCGATGCAGAAGTCACCGTTTATGAACGTAATGACGTGATCAGCTTCCTGTCTTGCGG TATTGCCCTGTACCTTGGAGGGAAGGTTGCCGACCCTCAGGGACTGTTCTATTCTTCTCCCGAAGAGCTGCAG AAACTGGGTGCAAATGTTCAGATGAACCACAATGTTCTGGCAATTGACCCCGACCAGAAAACTGTTACCGTAG AGGACCTCACTAATCATGCTCAGACTACCGAGTCGTACGACAAGCTGGTGATGACCTCTGGTTCTTGGCCTAT CGTCCCCAAGATTCCAGGTATCGACAGCGACCGCGTGAAGTTGTGCAAAAACTGGGCTCACGCTCAAGCACTG ATTGAGGACGCTAAGGAAGCAAAACGCATCACTGTTATCGGAGCTGGTTATATTGCTGCGGAGCTGGCAGAAG CGTATTCTACTACTGGACACGACGTTACCCTGATCGCACGTAGCGCACGCGTTATGCGTAAGTACTTCGATGC TGATTTCACTGACGTGATCGAACAGGATTATCGTGACCACGGTGTCCAGCTTGCTCTGGGAGAGACTGTGGAG TCCTTCACCGACTCTGCTACCGGACTGACTATCAAAACTGACAAGAACTCCTACGAGACTGATCTGGCTATCC TGTGCATAGGTTTTCGTCCCAACACCGACCTGCTTAAGGGTAAGGTTGACATGGCACCTAACGGAGCTATCAT CACTGATGACTACATGCGTTCCTCTAACCCCGATATTTTCGCCGCCGGTGATTCTGCCGCAGTTCATTATAAC CCCACTCACCAGAACGCATACATCCCACTGGCCACCAACGCTGTCCGTCAGGGCATCCTGGTCGGAAAGAACT TGGTCAAGCCAACGGTCAAATATATGGGAACACAAAGCTCTTCTGGTCTTGCACTTTACGATCGTACCATTGT TTCTACCGGACTGACCCTGGCTGCAGCTAAGCAGCAGGGTCTGAATGCAGAGCAGGTCATTGTCGAGGACAAT TACCGTCCTGAGTTTATGCCCAGCACTGAGCCAGTCTTGATGAGCCTTGTGTTCGATCCGGACACTCACCGCA TCCTGGGAGGTGCACTGATGTCAAAGTACGACGTTTCTCAATCTGCTAACACTCTGTCTGTTTGTATTCAGAA CGAGAATACTATTGACGACCTGGCTATGGTGGACATGCTGTTTCAGCCCAACTTTGATCGCCCCTTCAACTAC CTGAATATCCTGGCTCAGGCCGCACAGGCAAAGGTTGCACAATCGGTTAACGCAGGTGGTTCGGCTGTGAGCA AGGGCGAGGAGCTGTTCACCGGGGTGGTGCCCATCCTGGTCGAGCTGGACGGCGACGTAAACGGCCACAAGTT CAGCGTGTCCGGCGAGGGCGAGGGCGATGCCACCTACGGCAAGCTGACCCTGAAGTTCATCTGCACCACCGGC AAGCTGCCCGTGCCCTGGCCCACCCTCGTGACCACCCTGACCTACGGCGTGCAGTGCTTCAGCCGCTACCCCG ACCACATGAAGCAGCACGACTTCTTCAAGTCCGCCATGCCCGAAGGCTACGTCCAGGAGCGCACCATCTTCTT CAAGGACGACGGCAACTACAAGACCCGCGCCGAGGTGAAGTTCGAGGGCGACACCCTGGTGAACCGCATCGAG CTGAAGGGCATCGACTTCAAGGAGGACGGCAACATCCTGGGGCACAAGCTGGAGTACAACTACAACAGCCACA ACGTCTATATCATGGCCGACAAGCAGAAGAACGGCATCAAGGTGAACTTCAAGATCCGCCACAACATCGAGGA CGGCAGCGTGCAGCTCGCCGACCACTACCAGCAGAACACCCCCATCGGCGACGGCCCCGTGCTGCTGCCCGAC AACCACTACCTGAGTACTCAGTCCAAGCTGAGCAAAGACCCCAACGAGAAGCGCGATCACATGGTCCTGCTGG AGTTCGTGACCGCCGCCGGGATCACTCTCGGCATGGACGAGCTGTACAAATGA SEQ ID NO: 47 - The amino acid sequence of Arabidopsis thaliana oxygen evolving protein 23 transit peptide fused to Lactobacillus brevis NAD(P)H oxidase, containing mutations 159A / 177A / 178R / 179S / 184R, fused to monomeric enhanced GFP MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVS PADAGGMKVTVVGCTHAGTFAIKQILAEHPDAEVTVYERNDVISFLSCGIALYLGGKVADPQGLFYSSPEELQ KLGANVQMNHNVLAIDPDQKTVTVEDLTNHAQTTESYDKLVMTSGSWPIVPKIPGIDSDRVKLCKNWAHAQAL IEDAKEAKRITVIGAGYIAAELAEAYSTTGHDVTLIARSARVMRKYFDADFTDVIEQDYRDHGVQLALGETVE SFTDSATGLTIKTDKNSYETDLAILCIGFRPNTDLLKGKVDMAPNGAIITDDYMRSSNPDIFAAGDSAAVHYN PTHQNAYIPLATNAVRQGILVGKNLVKPTVKYMGTQSSSGLALYDRTIVSTGLTLAAAKQQGLNAEQVIVEDN YRPEFMPSTEPVLMSLVFDPDTHRILGGALMSKYDVSQSANTLSVCIQNENTIDDLAMVDMLFQPNFDRPFNY LNILAQAAQAKVAQSVNAGGSAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTG KLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIE LKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPD NHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK Detailed Description of the Invention The present invention will be described with respect to particular embodiments and with reference to certain drawings but the disclosure is not limited thereto but only by the claims. Any reference signs in the claims shall not be construed as limiting the scope. Of course, it is to be understood that not necessarily all aspects or advantages may be achieved in accordance with any particular embodiment. Thus, for example those skilled in the art will recognize that the disclosed embodiments may be embodied or carried out in a manner that achieves or optimizes one advantage or group of advantages as taught herein without necessarily achieving other aspects or advantages as may be taught or suggested herein. The disclosure, both as to organization and method of operation, together with features and advantages thereof, may best be understood by reference to the following detailed description when read in conjunction with the accompanying drawings. The aspects and advantages of the invention will be apparent from and elucidated with reference to the embodiment(s) described hereinafter. Reference throughout this specification to "one embodiment" or "an embodiment" means that a particular feature, structure or characteristic described in connection with the embodiment is included in at least one disclosed embodiment. Thus, appearances of the phrases "in one embodiment" or "in an embodiment" in various places throughout this specification are not necessarily all referring to the same embodiment, but may do so. Similarly, it should be appreciated that in the description of exemplary disclosed embodiments, various features are sometimes grouped together in a single embodiment, figure, or description thereof for the purpose of streamlining the disclosure and aiding in the understanding of one or more of the various inventive aspects. This method of disclosure, however, is not to be interpreted as reflecting an intention that the claimed invention requires more features than are expressly recited in each claim. Rather, as the following claims reflect, inventive aspects lie in less than all features of a single foregoing disclosed embodiment. It should be appreciated that “embodiments” of the disclosure can be specifically combined together unless the context indicates otherwise. The specific combinations of all disclosed embodiments (unless implied otherwise by the context) are further disclosed embodiments of the claimed invention. In addition, as used in this specification and the appended claims, the singular forms “a”, “an”, and “the” include plural referents unless the content clearly dictates otherwise. Thus, for example, reference to “a polynucleotide” includes two or more polynucleotides, reference to “a protein” includes two or more proteins, and the like. "About" as used herein when referring to a measurable value such as an amount, a temporal duration, and the like, is meant to encompass variations of ± 20 % or ± 10 %, more preferably ± 5 %, even more preferably ± 1 %, and still more preferably ± 0.1 % from the specified value, as such variations are appropriate to perform the disclosed methods. “Polynucleotide”, “nucleotide sequence”, “DNA sequence”, or “nucleic acid molecule(s)” as used herein refers to a polymeric form of nucleotides of any length, which comprises ribonucleotides or deoxyribonucleotides. This term refers only to the primary structure of the molecule. Thus, this term includes double- and single-stranded DNA, and RNA. The term “polynucleotide ” as used herein, may be a single or double stranded covalently-linked sequence of nucleotides in which the 3' and 5' ends on each nucleotide are joined by phosphodiester bonds. The polynucleotide may be made up of deoxyribonucleotide bases or ribonucleotide bases. Polynucleotides may be manufactured synthetically in vitro or isolated from natural sources. Polynucleotides may further include modified DNA or RNA, for example DNA or RNA that has been methylated, or RNA that has been subject to post-translational modification, for example 5’-capping with 7- methylguanosine, 3’-processing such as cleavage and polyadenylation, and splicing. Polynucleotides may also include synthetic nucleic acids (XNA), such as hexitol nucleic acid (HNA), cyclohexene nucleic acid (CeNA), threose nucleic acid (TNA), glycerol nucleic acid (GNA), locked nucleic acid (LNA) and peptide nucleic acid (PNA). The term “amino acid” in the context of the present disclosure is used in its broadest sense and is meant to include organic compounds containing amine (NH2) and carboxyl (COOH) functional groups, along with a side chain (e.g., an R group) specific to each amino acid. In some embodiments, the amino acids refer to naturally occurring L α- amino acids or residues. The commonly used one and three letter abbreviations for naturally occurring amino acids are used herein: A=Ala; C=Cys; D=Asp; E=Glu; F=Phe; G=Gly; H=His; I=Ile; K=Lys; L=Leu; M=Met; N=Asn; P=Pro; Q=Gln; R=Arg; S=Ser; T=Thr; V=Val; W=Trp; and Y=Tyr (Lehninger, A. L., (1975) Biochemistry, 2d ed., pp. 71-92, Worth Publishers, New York). The general term “amino acid” further includes D- amino acids, retro-inverso amino acids as well as chemically modified amino acids such as amino acid analogues, naturally occurring amino acids that are not usually incorporated into proteins such as norleucine, and chemically synthesised compounds having properties known in the art to be characteristic of an amino acid, such as β-amino acids. For example, analogues or mimetics of phenylalanine or proline, which allow the same conformational restriction of the peptide compounds as do natural Phe or Pro, are included within the definition of amino acid. Such analogues and mimetics are referred to herein as "functional equivalents" of the respective amino acid. Other examples of amino acids are listed by Roberts and Vellaccio, The Peptides: Analysis, Synthesis, Biology, Gross and Meiehofer, eds., Vol. 5 p. 341, Academic Press, Inc., N.Y. 1983, which is incorporated herein by reference. The terms “polypeptide” and “peptide” are interchangeably used herein to refer to a polymer of amino acid residues and to variants and synthetic analogues of the same. Thus, these terms apply to amino acid polymers in which one or more amino acid residues is a synthetic non-naturally occurring amino acid, such as a chemical analogue of a corresponding naturally occurring amino acid, as well as to naturally-occurring amino acid polymers. Polypeptides can also undergo maturation or post-translational modification processes that may include, but are not limited to: glycosylation, proteolytic cleavage, lipidization, signal peptide cleavage, propeptide cleavage, phosphorylation, and such like. A peptide can be made using recombinant techniques, e.g., through the expression of a recombinant or synthetic polynucleotide. A recombinantly produced peptide is typically substantially free of culture medium, e.g., culture medium represents less than about 20 %, more preferably less than about 10 %, and most preferably less than about 5 % of the volume of the protein preparation. The term “protein” is used to describe a folded polypeptide having a secondary or tertiary structure. The protein may be composed of a single polypeptide, or may comprise multiple polypeptides that are assembled to form a multimer. The multimer may be a homooligomer, or a heterooligomer. The protein may be a naturally occurring, or wild type protein, or a modified, or non-naturally, occurring protein. The protein may, for example, differ from a wild type protein by the addition, substitution or deletion of one or more amino acids. A “variant” of a protein encompasses peptides, oligopeptides, polypeptides, proteins and enzymes having amino acid substitutions, deletions and / or insertions relative to the unmodified or wild-type protein in question and having similar biological and functional activity as the unmodified protein from which they are derived. The term "amino acid identity" as used herein refers to the extent that sequences are identical on an amino acid-by-amino acid basis over a window of comparison. Thus, a "percentage of sequence identity" is calculated by comparing two optimally aligned sequences over the window of comparison, determining the number of positions at which the identical amino acid residue (e.g., Ala, Pro, Ser, Thr, Gly, Val, Leu, Ile, Phe, Tyr, Trp, Lys, Arg, His, Asp, Glu, Asn, Gln, Cys and Met) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison and multiplying the result by 100 to yield the percentage of sequence identity. For all aspects and embodiments of the present invention, a “variant” has at least 50%, 60%, 70%, 80%, 90%, 95% or 99% complete sequence identity to the amino acid sequence of the corresponding wild-type protein. Sequence identity can also be to a fragment or portion of the full-length polynucleotide or polypeptide. Hence, a sequence may have only 50 % overall sequence identity with a full-length reference sequence, but a sequence of a particular region, domain or subunit could share 80%, 90%, or as much as 99% sequence identity with the reference sequence. The term “wild-type” refers to a gene or gene product isolated from a naturally occurring source. A wild-type gene is that which is most frequently observed in a population and is thus arbitrarily designed the “normal” or “wild-type” form of the gene. In contrast, the term “modified”, “mutant” or “variant” refers to a gene or gene product that displays modifications in sequence (e.g., substitutions, truncations, or insertions), post-translational modifications and / or functional properties (e.g., altered characteristics) when compared to the wild-type gene or gene product. Methods for introducing or substituting naturally-occurring amino acids are well known in the art. For instance, methionine (M) may be substituted with arginine (R) by replacing the codon for methionine (ATG) with a codon for arginine (CGT) at the relevant position in a polynucleotide encoding the mutant monomer. Methods for introducing or substituting non-naturally-occurring amino acids are also well known in the art. For instance, non-naturally-occurring amino acids may be introduced by including synthetic aminoacyl-tRNAs in the IVTT system used to express the mutant monomer. Alternatively, they may be introduced by expressing the mutant monomer in E. coli that are auxotrophic for specific amino acids in the presence of synthetic (i.e. non-naturally-occurring) analogues of those specific amino acids. They may also be produced by naked ligation if the mutant monomer is produced using partial peptide synthesis. Conservative substitutions replace amino acids with other amino acids of similar chemical structure, similar chemical properties or similar side-chain volume. The amino acids introduced may have similar polarity, hydrophilicity, hydrophobicity, basicity, acidity, neutrality or charge to the amino acids they replace. Alternatively, the conservative substitution may introduce another amino acid that is aromatic or aliphatic in the place of a pre-existing aromatic or aliphatic amino acid. Conservative amino acid changes are well-known in the art and may be selected in accordance with the properties of the 20 main amino acids as defined in Table 1 below. Where amino acids have similar polarity, this can also be determined by reference to the hydropathy scale for amino acid side chains in Table 2. Table 1 - Chemical properties of amino acids Ala aliphatic, hydrophobic, neutral Met hydrophobic, neutral Cys polar, hydrophobic, neutral Asn polar, hydrophilic, neutral Asp polar, hydrophilic, charged (-) Pro hydrophobic, neutral Glu polar, hydrophilic, charged (-) Gln polar, hydrophilic, neutral Phe aromatic, hydrophobic, neutral Arg polar, hydrophilic, charged (+) Gly aliphatic, neutral Ser polar, hydrophilic, neutral His aromatic, polar, hydrophilic, Thr polar, hydrophilic, neutral charged (+) Ile aliphatic, hydrophobic, neutral Val aliphatic, hydrophobic, neutral Lys polar, hydrophilic, charged(+) Trp aromatic, hydrophobic, neutral Leu aliphatic, hydrophobic, neutral Tyr aromatic, polar, hydrophobic Table 2 - Hydropathy scale __________________________________ Side Chain Hydropathy ______________________________________ Ile 4.5 Val 4.2 Leu 3.8 Phe 2.8 Cys 2.5 Met 1.9 Ala 1.8 Gly -0.4 Thr -0.7 Ser -0.8 Trp -0.9 Tyr -1.3 Pro -1.6 His -3.2 Glu -3.5 Gln -3.5 Asp -3.5 Asn -3.5 Lys -3.9 Arg -4.5 _______________________________________________ Unless otherwise indicated, nucleic acid sequences herein are written in the 5’-to- 3’ direction from left to right. As used herein, a “recombinant cell” will be understood to mean a cell into which a recombinant nucleic acid (e.g. recombinant DNA, recombinant RNA) has been introduced. A “recombinant nucleic acid” is a nucleic acid sequence comprising a combination of nucleic acid molecules that would not otherwise exist in nature. Recombinant nucleic acids as referred to herein may be synthesised recombinant nucleic acids. As used herein, a water-forming NADH or NADPH oxidase will be understood to refer to an enzyme that can reduce molecular oxygen to form water through oxidation of NADH or NADPH. Any such enzyme may also produce other products such as H2O2. Many such proteins are known to those of ordinary skill in the art and the proteins have been identified in bacteria (Higuchi M, et al 1993 The Journal of General Microbiology. 139, 2343–2351. doi: 10.1099 / 00221287-139-10-2343), archaea (Ward D.E., FEBS J. 2001268:5816–5823. doi: 10.1046 / j.0014-2956.2001.02526.x.), and eukaryotes (Brown D.M., et al 1996 European journal of biochemistry, 241(1), pp.155-161). It would be expected that any water-forming oxidase would function equivalently as it is the enzyme activity, and not the sequence identity, that provides utility in the invention. A person of ordinary skill in the art would be able to use sequence search methods such as BLAST (Altschul et al J. Mol Biol 1990215(3):403-410), hmmer (Eddy S. Bioinformatics 1998 14(9):755-763) or orthology inference methods such as OrthoFinder (Emms D.M et al 2019 Genome Biology 20:238), or OrthoMCL (Li et al 2003 Genome Research 13(9): 2178-2189) to identify sequences related to known water-forming oxidases and then confirm their function as water-forming NADH or NADPH oxidase through enzymatic characterisation. It will be appreciated by persons of ordinary skill in the art that other water-forming NADH or NADPH oxidase genes not listed in this invention will provide the same biochemical function, and thus will provide the same effect if expressed in plant cells in the same manner as the examples provided herein. As used herein, NOX is used as an abbreviation to refer to a water-forming NADH or NADPH oxidase. For example, SmNOX refers to bifunctional the water-forming NADPH and NADH oxidase from Streptococcus mutans [SEQ ID NO: 18]. LbNOX refers to the water-forming NAD(P)H oxidase from Lactobacillus brevis [SEQ ID NO: 14]. As used herein, the terms “overexpress”, “overexpressed” and “overexpression” in the context of expressing a given biological entity (e.g. nucleic acid, protein, peptide and the like) in a recombinant cell refers to: (i) expression of the entity in the recombinant cell at a level greater than a level of expression of the same entity in a corresponding wild-type cell; or (ii)expression of the entity in the recombinant cell at a detectable level when a corresponding wild-type cell expresses the same entity at non-detectable levels, or does not express the entity at all. As used herein, the term “corresponding wild-type” in the context of modified cells, organisms, nucleic acid sequences, proteins, peptides and the like refers to the natural form of the entity. For example, in the case of a recombinant cell engineered to contain a vector comprising an exogenous nucleic acid sequence, the “corresponding wild- type” cell would be the cell as it existed in natural form prior to having been engineered to include the vector. By way of further non-limiting example, the “corresponding wild-type” of a codon-optimised nucleic acid or amino acid sequence would be the sequence as it existed in natural form prior to the codon optimisation. As used herein, a “C3photosynthetic plant”, will be understood to encompass any plant in which all or the majority of photosynthesis is C3photosynthesis. “C3photosynthesis” means a photosynthetic pathway which uses the Calvin-Benson cycle to fix carbon dioxide from air without additional biophysical or biochemical mechanisms to concentrate that CO2. Cell types referred to herein as “C3” will be understood to be from a “C3photosynthetic plant”. As used herein, a “C4photosyntheic plant”, will be understood to encompass any plant in which all or the majority of photosynthesis is C4photosynthesis. Cell types referred to herein as “C4” will be understood to be from a “C4photosynthetic plant”. As used herein, a “plant part” may be a fruit, a leaf, a root, or plant vasculature (e.g. xylem). Fruit comprises tissues such as fruit flesh and fruit peel. The “plant part” may be a seed. The term “seed” as used herein may refer to a unit of reproduction of a flowering plant capable of developing into another such plant. The term “plant organ” refers to plant tissue or a group of tissues that constitute a morphologically and functionally distinct part of a plant. The term “genome” refers to the entire complement of genetic material (genes and non-coding sequences) that is present in each cell of an organism, or virus or organelle; and / or a complete set of chromosomes inherited as a (haploid) unit from one parent. “Progeny” comprises any subsequent generation of a plant. As used herein, a percentage of “sequence identity” will be understood to arise from a comparison of two sequences in which they are aligned together to give a maximum correlation between the sequences. This may include inserting “gaps” in either one or both sequences to enhance the degree of alignment. The percentage of sequence identity may then be determined over the length of each of the sequences being compared. For example, a nucleotide sequence (“subject sequence”) having at least 95% “sequence identity” with another nucleotide sequence (“query sequence”) is intended to mean that the subject sequence is identical to the query sequence except that the subject sequence may include up to five nucleotide alterations per 100 nucleotides of the query sequence. In other words, to obtain a nucleotide sequence of at least 95% sequence identity to a query sequence, up to 5% (i.e. 5 in 100) of the nucleotides in the subject sequence may be inserted or substituted with another nucleotide or deleted. Percentage identity is also used equivalently in relation to protein sequences but in terms of comparing the corresponding amino acids. As used herein, a regulatory sequence “operably linked” to another sequence means that a functional relationship exists between the two sequences such that the regulatory sequence has the capacity to exert an influence on the expression and / or localisation and / or activity of the sequence to which it is linked. For example, a promoter operably linked to a coding sequence will be capable of modulating the transcription of that coding sequence. A targeting peptide or N-terminal or C-terminal fusion protein operably linked to a polypeptide will be capable of directing the polypeptide to a specific location (e.g. an organelle or cytoplasmic membrane). As used herein, photosynthetically active cells are defined as any cell within a plant that is capable of fixing atmospheric CO2into sugars using energy obtained from light. In most plants the primary photosynthetically active cells are the mesophyll cells of the leaf. In leaves there can be multiple mesophyll cell layers including but not limited to spongy mesophyll cell layers and palisade mesophyll cell layers. The term mesophyll cells as used herein encompasses all types of mesophyll cell and mesophyll cell layer unless the context clearly dictates otherwise. Furthermore, as used herein, the term mesophyll cell promoter or promoter that is active in photosynthetically active tissue refers to any promoter that is capable of driving expression of a gene in a mesophyll cell or a photosynthetically active cell. Many such promoters are known to those of ordinary skill in the art. It would be expected that the promoter of any gene that is expressed in mesophyll cells and / or photosynthetically active cells when fused to a target gene would direct expression of that target gene in mesophyll cells and / or photosynthetically active cells. Many such mesophyll cell promoters have been characterized in the literature including but not limited to the promoters for the following genes. Rubisco small subunit (pRBCS1A): Mustroph, et al 2009 PNAS 106 (44): 18843-18848. Chlorophyll a / b-binding protein (cab) promoters: Mitra et al. 1989 Plant Molecular Biology 12: 169-179, 1989. PEPC: Das Gupta et al. 2019 The Plant Journal 101 (1): 204-216. IQD22: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. AT1G70958: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. SQE6: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. XTH6: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. PAL1: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. CORI3: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. YAB3: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. LHCB2.4: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. CRR23: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. SPS4F: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. ENH1: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. COR414-TM1: Procko et al 2022 The Plant Cell 34 (9): 3261–3279. Features, integers, characteristics, compounds, chemical moieties or groups described in conjunction with a particular aspect, embodiment or example of the invention are to be understood to be applicable to any other aspect, embodiment or example described herein unless incompatible therewith. All of the features disclosed in this specification (including any accompanying claims, abstract and drawings), and / or all of the steps of any method or process so disclosed, may be combined in any combination, except combinations where at least some of such features and / or steps are mutually exclusive. The invention is not restricted to the details of any foregoing embodiments. The invention extends to any single feature, or any novel combination, of the features disclosed in this specification (including any accompanying claims, abstract and drawings), or to any novel single feature, or any novel combination, of the steps of any method or process so disclosed. Polynucleotide Provided here is a novel approach for enhancing plant growth and yield. This is achieved through the engineering of plants to contain a polynucleotide comprising a promoter element operatively linked to a nucleotide sequence that encodes a water- forming oxidase. The polynucleotide may advantageously enhance plant growth and yield by altering the relative concentration of CO2and O2in proximity to rubisco in the chloroplast, thereby reducing the occurrence of photorespiration. The invention may be particularly advantageous in numerous applications including, but not limited to, industrial biotechnology (wherein enhanced growth and / or yield would result in enhanced production of proteins, peptides, metabolites, molecules, compounds, and the like), and in food, feed, biomass and biofuel production (wherein enhanced growth and / or yield would result in enhanced production of food, feed, biomass or biofuel). As explained in more detail herein, provided is a polypeptide capable of enhancing plant growth and yield in a plant comprising said polypeptide. Provided herein is a polynucleotide comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. Promoter element A promoter, or promoter element is a sequence capable of driving expression of an operatively linked gene. The promoter element may comprise, or be derived from, or consist of the promoter of any gene expressed in plant cells. The promoter element is preferably capable of driving expression of a gene in a photosynthetic cell, more preferably in a mesophyll cell. A transcription factor activated promoter may also be used, such as STAP (Brückner K. et al 2015 Plant Journal. 82: 707 – 716) or those described in Lie et al 2016 Current Opinion in Biotechnology. 37:36-44. Or any multiplicity of target gene sequences can each be independently linked to respective such promoters, whether fused or linked in series or otherwise connected. Transcription factor activated promoter(s) may be operably linked to at least one transcription factor such as dTALE (See Brückner K. et al (2015) Plant Journal. 82: 707 - 716.), or may be linked to a promoter that is active in photosynthetically active cells. The promoter element may therefore comprise, or be derived from, or consist of the promoter of a gene ubiquitously expressed in all plant cells, a gene expressed in a mesophyll cell or a gene expressed in a photosynthetically active cell. The gene is preferably expressed in C3 plant cells. Alternatively, the promoter element may comprise, or be derived from, or consist of the promoter of a tissue-specific promoter, such as of a gene that is expressed only in photosynthetically active cells or mesophyll cells. The plant cell promoter element may be derived from, or consist of, but not limited to one of the following gene promoters: rubisco small subunit (pRBCS1A), Chlorophyll a / b-binding protein (cab), and more preferably the CAB3 promoter, PEPC, IQD22, AT1G70958, SQE6, XTH6, PAL1, CORI3, YAB3, LHCB2.4, CRR23, SPS4F, ENH1, or COR414-TM. The plant cell promoter element may be derived from, or consist of, a promoter of a gene expressed, or specifically expressed, in a cell of a plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the cell is a stomatal progenitor cell. The skilled person would understand that a stomatal progenitor cell is an undifferentiated leaf epidermal cell prior to the onset or completion of stomatal lineage differentiation. As would be appreciated by a person skilled in the art, stomatal progenitor cells may be identified by their expression of SPCH, MUTE and FAMA genes. The promoter element may be any sequence of a known promoter that is capable of driving expression of the gene to which it isoperatively linked. The promoter element is therefore not limited according to its sequence length. For example, the promoter element may comprise or consist of the minimum one or more transcription factor binding sites necessary for the induction of transcription of the operatively linked nuceleotide sequence. A person skilled in the art would understand how to engineer a plant cell promoter that comprises, is derived from, or consists of the promoter of a given gene such that the operatively linked nucleotide sequence may be transcribed in a given organism. Any of the promoter elements described herein may be ubiquitously active or may be inducible. A person skilled in the art would understand how to derive or engineer a plant cell promoter element such that it is ubiquitously active or inducible. Water-forming oxidase The sequence that encodes the water-forming oxidase comprised in the polynucleotide described herein may be modified to enhance expression in plants or plant cells. Many publicly available online tools exist to enable the skilled artisan to optimise a nucleotide or protein sequence for use in the present invention (see, for example, http: / / genomes.urv.es / OPTIMIZER). Preferably, the sequence is codon-optimised, e.g. for expression in plants or in particular genera or species of plants. As known to those of skill in the art, organisms differ in their tendency to use specific codons over others to encode the same amino acid. A codon-optimised sequence may therefore enhance the expression of the water-forming oxidase in plants, or in specific genera or species of plants or in specific cell types. The sequence encoding the water-forming oxidase may be modified by the addition or removal of one or more introns. The sequence encoding the water-forming oxidase may be modified by operably linking it to further regulatory sequences in addition to the plant cell promoter element (e.g. enhancers and the like) to further manipulate the level at which they are transcribed. Preferably the water-forming oxidase is an NADPH water-forming oxidase, an NADH water-forming oxidase, or a bifunctional NAD(P)H water-forming oxidase. The sequence encoding the water-forming oxidase may be derived from any suitable source organism. The sequence encoding the water-forming oxidase may particularly be derived from any bacterial species, such as Streptococcus mutans and Lactobacillus brevis. The water-forming oxidase may be encoded by a nucleotide sequence comprising or consisting of the sequence defined according to SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO:36, SEQ ID NO: 38. SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, or SEQ ID NO: 46, or a variant thereof. The variant may have at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 87%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO:36, SEQ ID NO: 38. SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, or SEQ ID NO: 46. The variant may be an enzymatically active variant, namely wherein the variant retains the enzymatic function of a water-forming oxidase as described herein. The water-forming oxidase may comprise or consist of the sequence defined according to SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO:37, SEQ ID NO: 39. SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45, or SEQ ID NO: 47, or a variant thereof. The variant may comprise or consist of an amino acid sequence having at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 87%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO:37, SEQ ID NO: 39. SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45, or SEQ ID NO: 47. The variant may be an enzymatically active variant namely wherein the variant retains the enzymatic function of a water-forming oxidase as described herein. More preferably, the water-forming oxidase may be encoded by a sequence comprising or consisting of the sequence defined according to SEQ ID NO: 14, SEQ ID NO: 16 or SEQ ID NO: 18, or a variant thereof. The variant may comprise or consist of a sequence having at least, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 87%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity to SEQ ID NO: 14, SEQ ID NO: 16 or SEQ ID NO: 18. The water-forming oxidase may comprise or consist of the sequence defined according to SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, or a variant thereof. The variant may comprise or consist of a sequence having at least, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 87%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity to SEQ ID NO: 15, SEQ ID NO: 17 or SEQ ID NO: 19. The polynucleotide may preferably further comprise a terminator sequence, preferably wherein the terminator sequence is 3’ relative to the sequence encoding the water-forming oxidase. A person of skill in the art would understand that any terminator capable of terminating transcription may be suitably comprised in the polynucleotide provided herein. The terminator sequence may for example be nopaline synthase terminator (NOSt) terminator (SEQ ID NO: 3). The nucleotide sequence operatively linked to plant cell promoter element may further encode one or more of: i. a protein that differs from the water-forming oxidase; ii. a target peptide; and iii. a transmembrane protein or domain, optionally wherein the one or more of i. to iii. are separated from the water-forming oxidase by a linker. The i. to iii. and the linker are all preferably encoded in-frame with the water- forming oxidase, and are thereby translationally (i.e. genetically) fused. i. to iii. may be encoded 5’ to the water-forming oxidase, thereby resulting in their fusion to the N- terminus of the water-forming oxidase. i. to iii. may be encoded 3’ to the water-forming oxidase, thereby resulting in their fusion to the C-terminus of the water-forming oxidase. The protein that differs from the water-forming oxidase may for example be a protein which localises to a particular sub-cellular or extra-cellular location. As a consequence, following expression of the water-forming oxidase encoded by the polynucleotide provided herein, the water-forming oxidase will necessarily become localised to the typical sub-cellular or extra-cellular location of the protein that differs from the water-forming oxidase. The protein according to i. may for example the protein encoded by the rubisco small subunit gene (see for example the encoding sequence of SEQ ID NO: 6) which is targeted to the chloroplast of a plant cell. The protein that differs from the water-forming oxidase may for example be a protein which allows the identification of the expression of the water-forming oxidase, for example a fluorescent protein which can be visualised by fluorescence microscopy. The protein according to i. may for example be green fluorescent protein (GFP), preferably wherein the protein is fused to the C-terminus of the water-forming oxidase. The target peptide according to ii. may be any peptide sequence known to target a protein to a particular sub-cellular or extra-cellular location. The peptide encompasses known transit peptides, localisation sequences and signal peptides. For example, the peptide sequence may be a chloroplast transit peptide, peroxisomal targeting sequence, nuclear localisation sequence, mitochondrial transit peptide, endosomal targeting peptide, signal peptide or any other cellular targeting peptide. The protein according to ii. may for example be the chloroplast transit peptide from the oxygen evolving protein 16 gene (see for example the sequence encoding said chloroplast transit peptide in SEQ ID NO: 8). The protein according to ii. may alternatively be the chloroplast transit peptide from the oxygen evolving protein 23 gene (see for example the sequence encoding said chloroplast transit peptide in SEQ ID NO: 11). The transmembrane protein or domain according to iii. may enable localisation to any membrane within a cell or to the extracellular membrane. A skilled person would be able to identify suitable proteins or domains and engineer encoding sequences to ensure the localisation of the water-forming oxidase to a desired location in a cell. The transmembrane protein according to iii. may, for example, be the protein encoded by the outer envelope protein 9 gene (see for example SEQ ID NO 12) which localises to the outer envelope of chloroplasts. The nucleotide sequence encoding the water-forming oxidase is preferably separated from the sequence encoding any one or more of i. to iii. by a sequence encoding a linker. The linker may be any suitable linker known to a person skilled in the art. The linker may be flexible or rigid. Preferred flexible peptide linkers are stretches of 2 to 40, such as 2 to 20, such as 4, 6, 8, 10 or 16, serine and / or glycine amino acids. More preferred flexible linkers include (SG)1, (SG)2, (SG)3, (SG)4, (SG)5 and (SG)8 wherein S is serine and G is glycine. A yet more preferred flexible linker is a poly-Glycine-Serine linker such as GGGGSGGGGS. Preferred rigid linkers are stretches of 2 to 30, such as 4, 6, 8, 16 or 24, proline amino acids. More preferred rigid linkers include (P)12 wherein P is proline. A more preferred rigid linker is an amino acid sequence AEAAAKEAAAKEAAAKA. Vector Provided herein is a vector comprising the polynucleotide of the invention. Such expression vectors are routinely constructed in the art of molecular biology and may for example involve the use of plasmid DNA and appropriate initiators, promoters, enhancers and other elements, such as for example polyadenylation signals which may be necessary, and which are positioned in the correct orientation, in order to allow for expression of a peptide of the invention. The vector may also encode a further fluorescent protein aside from any fluorescent protein expressed in frame with the water-forming oxidase, wherein said further fluorescent protein is separated from the nucleotide sequence of the polynucleotide of the invention by an internal ribosomal entry site (IRES) or under the control of an additional promoter. The vector preferably comprises an origin of replication, and a T-DNA right border repeat of a Ti or Ri plasmid, optionally further comprising a left border repeat of a Ti or Ri plasmid, and at least one bacterial selectable marker. The vector may comprise one or more of: i.an enhancer; ii. a plant selectable marker; iii. a multicloning site; and iv. a recombination site. Suitable vectors for this purpose are well known to those of skill in the art and include, without limitation, plasmids, cosmids, vectors, artificial chromosomes, modified viruses, and mobile genetic elements. Other suitable vectors would be apparent to persons skilled in the art. By way of further example in this regard we refer to Sambrook et al. (Sambrook, J., Fritsch, E. R., & Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press). Composition and transformation Provided herein is a composition for transforming plant cells, the composition comprising a polynucleotide according to the invention and / or a vector according to the invention, preferably wherein the composition comprises a microparticle complexed with the polynucleotide and or the vector or wherein the polynucleotide and or the vector is transformed into plant cells using agrobacterium mediated transformation. Transformation of plants is now a routine technique for a person skilled in the art. Advantageously, any of the composition provided herein can be subject to any suitable transformation methods in order to introduce the polynucleotide and / or vector into a suitable ancestor cell. The composition may comprise any known components that renders the composition suitable for the described methods for the transformation and regeneration of plants from plant tissues or plant cells, wherein said composition may be utilized for transient or for stable transformation. Transformation methods include the use of liposomes, electroporation, chemicals that increase free DNA uptake, injection of the DNA directly into the plant, particle gun bombardment, agrobacterium mediate transformation, transformation using viruses or pollen, or microprojection. Methods may be selected from the calcium / polyethylene glycol method for protoplasts, electroporation of protoplasts, microinjection into plant material, DNA or RNA-coated particle bombardment, infection with (non-integrative) viruses and the like. Methods for coating DNA or RNA onto microparticles are well known to those of ordinary skill in the art for example the methods described in Ismagul et al BMC Plant Biology 201818: 135, or Kikkert JR. Cell biology: a laboratory handbook, vol. 4. San Diego: Academic Press; 1998. p. 157–61, or Sanford JC, et al. Methods Enzymol. 1993217:483–509. Accordingly, suitable microparticles complexed with the polynucleotide and / or the vector of the composition are known to the skilled person. Methods of the invention that comprise modifying heritable genetic material of a plant may comprise transforming the plant, preferably wherein the transforming comprises Agrobacterium mediated transformation. Transgenic plants, including transgenic crop plants, are preferably produced via Agrobacterium tumefaciens mediated transformation. Methods of the invention that comprise modifying heritable genetic material of a plant may comprise any suitable transformation method known in the art including any process of transformation described herein. Preferably, the step of modifying the heritable genetic material of a plant in any of the methods provided herein does not comprise an essentially biological process, e.g. does not comprise crossing and selection. Transformation methods are well known in the art. Thus, according to the various aspects of the invention, a composition and / or polynucleotide of the invention may be introduced into a plant such that the polynucleotide and / or vector is expressed as a transgene. Nucleic acids are introduced into a plant through transformation. The term "introduction" or "transformation" as referred to herein encompasses the transfer of an exogenous polynucleotide into a host cell, irrespective of the method used for transfer. Plant tissue capable of subsequent clonal propagation, whether by organogenesis or embryogenesis, may be transformed with a genetic construct of the present invention and a whole plant regenerated there from. The particular tissue chosen will vary depending on the clonal propagation systems available for, and best suited to, the particular species being transformed. Exemplary tissue targets include leaf disks, pollen, embryos, cotyledons, hypocotyls, megagametophytes, callus tissue, existing meristematic tissue (e.g., apical meristem, axillary buds, and root meristems), and induced meristem tissue (e.g., cotyledon meristem and hypocotyl meristem). The polynucleotide and / or vector may be transiently or stably introduced into a host cell and may be maintained non-integrated, for example, as a plasmid. Alternatively, it may be integrated into the host genome. The resulting transformed plant cell may then be used to regenerate a transformed plant in a manner well known in the art. To select transformed plants, plant material obtained in the transformation is, as a rule, subjected to selective conditions so that transformed plants can be distinguished from untransformed plants. For example, seeds obtained in the above-described manner can be planted and, after an initial growing period, subjected to a suitable selection by spraying. A further possibility is growing the seeds, if appropriate after sterilization, on agar plates using a suitable selection agent so that only the transformed seeds can grow into plants. Alternatively, the transformed plants are screened for the presence of a selectable marker either visually using fluorescent of color based reporters, or using molecular techniques to detect the presence of the polynucleotide of the invention. Following DNA transfer and regeneration, putatively transformed plants may also be evaluated, for instance using Southern blot analysis or PCR analysis, for the presence of the gene of interest, copy number and / or genomic organisation. Alternatively or additionally, expression levels of the newly introduced DNA may be monitored using Northern and / or Western analysis, or by rtPCR or RNA-Seq all such techniques being well known in the art. The generated transformed plants may be propagated by a variety of means, such as by clonal propagation or classical breeding techniques. For example, a first generation (or T1) transformed plant may be selfed and homozygous second-generation (or T2) transformants selected, and the T2 plants may then further be propagated through classical breeding techniques. The generated transformed organisms may take a variety of forms. For example, they may be chimeras of transformed cells and non-transformed cells; clonal transformants (e.g., all cells transformed to contain the expression cassette); grafts of transformed and untransformed tissues (e.g., in plants, a transformed rootstock grafted to an untransformed scion). Altered plants in accordance with the invention advantageously provide better yield characteristics. Yield characteristics, also known as yield traits may comprise one or more of the following non-limitative list of features: yield, biomass, seed yield, seed / grain size, starch content of grain, early vigour, greenness index, Landsat Normalized Difference Vegetation Index, increased growth rate, early flowering, enhanced resilience to environmental variation. The term "yield" in general means a measurable produce of economic value, typically related to a specified crop, to an area, and to a period of time. Individual plant parts directly contribute to yield based on their number, size and / or weight. The actual yield is the yield per square meter for a crop and year, which is determined by dividing total production (includes both harvested and appraised production) by planted square metres. The term "yield" of a plant may relate to vegetative biomass (root and / or shoot biomass), to reproductive organs, and / or to propagules (such as seeds) of that plant. Thus, according to the invention, yield comprises one or more of and can be measured by assessing one or more of: increased seed yield per plant, increased seed filling rate, increased number of filled seeds, increased harvest index, increased viability / germination efficiency, increased number or size of seeds / capsules / pods, increased growth, increased seed number, increased number of floral organs, increased biomass or increased grain fill. Preferably, increased yield comprises an increased number of grains / seeds / capsules / pods, increased biomass, increased growth, and / or increased number of floral organs. Yield is usually measured relative to a control plant. Cell Provided herein is a cell comprising the polynucleotide according to the invention or vector according to the invention. The cell may be any cell suitable for cloning, for example a bacterial cell, preferably wherein the bacterial species is E. coli, Agrobacterium sp. or A. tumefaciens. The cell may be a plant cell, such as a C3plant mesophyll cells, a C3plant vascular sheath cell, a C3plant bundle sheath cell, a C3plant mestome sheath cell, a C4photosynthetic plant cell such as a C4plant vascular sheath cell, a C4plant bundle sheath cell, a C4plant mestome sheath cell or a C4plant mesophyll cell; or a CAM photosynthetic plant cell, such as a CAM plant vascular sheath cell, a CAM plant bundle sheath cell, a CAM plant mestome sheath cell or a CAM plant mesophyll cell. The cell is preferably a plant cell, wherein the plant cell is capable of undertaking photosynthesis and / or is preferably a C3plant cell. The cell may be a C3or C4plant cell, preferably wherein the cell is a cell of a plant leaf epidermis and / or is capabale of undertaking photosynthesis, preferably wherein the cell is a stomatal cell, and more preferably wherein the stomatal cell is a stomatal progenitor cell. The cell may be a photosynthetic cell which may be a photosynthetic bacterium (such as a cyanobacterium) or a photosynthetic algal cell (such as those found in chlorophyte or streptophye algae) The plant cell may be any of plant tissue such as leaf disks, pollen, embryos, cotyledons, hypocotyls, megagametophytes, callus tissue, existing meristematic tissue (e.g., apical meristem, axillary buds, and root meristems), and induced meristem tissue (e.g., cotyledon meristem and hypocotyl meristem). The plant cell is preferably a mesophyll cell, a stomatal cell, or a stomatal progenitor cell. Most preferably, the plant cell is a stomatal progenitor cell. The cell with modified genetic material according to the method herein may be used in biological production given that they provide a means of enhancing growth and / or biomass. For example, the cells of the present invention can be used in the commercial production of specialty metabolites isolated from plant cells, which may in turn be used as building blocks for a large range of complex chemicals, non-limiting examples of which include polymers, solvents and pharmaceuticals. Further methods of the present invention involve the generation of transgenic plants as described herein. The transgenic plants will have an increased growth rate or biomass as compared to a corresponding wild-type plant. Plant Provided herein is a plant or part thereof comprising: i. a cell according to the invention; or ii. a cell comprising a polynucleotide which comprises a promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The promoter element of the cell of ii. may be any promoter element capable of driving expression of an operatively linked gene and is not limited to a plant cell promoter element. The promoter element may comprise, be derived from, or consist of, any suitable promoter known the skilled person. For example, the promoter element may be synthetic, or composed of minimal elements, or come from non-plant hosts (such as the CaMV 35S promoter). The promoter element may otherwise be defined according to the promoter element of the polynucleotide provided herein. The plant provided herein is preferably a transgenic plant. The plant provided herein preferably has enhanced growth compared to a control unmodified plant grown under the same conditions, preferably wherein the plant is a C3or C4plant, preferably wherein the conditions are water-deficit conditions. The skilled person understands conditions which define water-deficit conditions in the context of plant growth. Water deficit conduitions occur in agricultural or natural environments and occur under any condutions where water availability is limiting to photosynthesis or growth. Water deficit conditions may also comprise cultivating the plant in water-deficient growth media. For example, in some assays, water-deficit conditions may be maintained by providing water to a growth medium (e.g. soil), but then with-holding water over a prolonged period to maintain sub-optimal and deteriorating growth medium-water saturation levels during growth. For example, water-deficit conditions may be maintained by providing water to a growth medium (e.g. soil) prior to seed stratification, but water is then withheld for 15- days after the termination of stratification to maintain sub-optimal and deteriorating growth medium-water saturation levels during vegetative growth. The plant may be a monocot plant and may, for example, be selected from the families Arecaceae, Amaryllidaceae or Poaceae. For example, the plant may be a cereal crop, such as wheat, rice, barley, oat, triticale, rye, buckwheat, or a non-cereal monocot crop such as garlic, onion, leek, yam, oil palm, or banana. The plant may be a dicot plant and may, for example, be selected from the families Asteraceae, Brassicaceae (e.g. Brassica napus), Chenopodiaceae, Cucurbitaceae, Leguminosae (Caesalpiniaceae, Aesalpiniaceae Mimosaceae, Papilionaceae or Fabaceae), Malvaceae, Rosaceae or Solanaceae. For example, the plant may be selected from lettuce, sunflower, broccoli, spinach, water melon, squash, cabbage, tomato, potato, sweet potato, capsicum, tobacco, cotton, okra, apple, rose, strawberry, alfalfa, bean, soybean, field (fava) bean, pea, lentil, peanut, chickpea, apricots, pears, peach, grape vine, bell pepper, chilli, citrus or coffee species. The plant may be a biofuel or bioenergy crop such as rape / canola, linseed, lupin and willow, poplar, poplar hybrids, or gymnosperms, such as loblolly pine. Also included are crops for silage, grazing or fodder (grasses, clover, sanfoin, alfalfa), fibres (e.g. hemp, cotton, flax), building materials (e.g. pine, oak, teak, rosewood), pulping (e.g. poplar), feeder stocks for the chemical industry (e.g. high erucic acid oil seed rape, linseed, jute, oil palm). The plant is most preferably a C3plant. The C3plant is preferably a crop plant, particularly wherein the crop plant is capable of being commercially for human or animal consumption or use. Preferably, the crop plant is a cereal plant, an oilseed plant or a legume plant. The C3plant provided herein may for example be Soy (Glycine max), cotton (Gossypium hirsutum), oilseed rape / Cannola (B. napus subsp. Napus), potato (Solanum tuberosum), tomato (Solanum lycopersicum), wheat (Triticum aestivum), barley (Hordeum vulgare), oat (Avena sativa), rice (Oryza sativa), rye (Secale cereal), pigeon pea (Cajanus cajan), cowpea (Vigna unguiculata), pea (Pisum sativum), sugar beet (Beta vulgaris), Castor oil (Ricinus communis), cassava (Manihot esculenta), sweet potato (Ipomoea batatas), yam (Dioscorea spp.), peanut (Arachis hypogaea), Sunflower (Helianthus annuus), flax (Linum spp.), beans (Phaseolus vulgaris), lima bean (Phaseolus lunatus), mung bean (Phaseolus mung), Adzuki bean (Phaseolus angularis), chickpea (Cicer arietinum), buckwheat (Fagopyrum esculentum), tobacco (Nicotiana tabacum), cannabis (Cannabis sativa), oil palm (Elaeis guineensis), Sycamore (Acer pseudoplatanus), Sweet chestnut (Castanea sativa), Poplar (Populus spp.), Eucalyptus (Sucalyptus spp.), Plantain / banana (Musa acuminate), or rubber (Hevea brasiliensis) plant. The plant part provided herein may be any part of a C3plant. For example, the plant part may be a seed, a fruit, a shoot, a stem, a leaf, a root (including tubers), a flower, a tissue or an organ. The plant is a also preferably a C4plant. The C4plant is preferably a crop plant, particularly wherein the crop plant is capable of being commercially for human or animal consumption or use. The C4plant provided herein may for example be a maize (Zea mays), Sorghum (Sorghum bicolor), Sugar cane, Teff, Millets, or other C4herbs, grasses or cereals. The plant part provided herein may be any part of a C4plant. For example, the plant part may be a seed, a fruit, a shoot, a stem, a leaf, a root (including tubers), a flower, a tissue or an organ. A method and product thereof Provided herein is a method for increasing growth and yield of a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one mesophyll cell of the plant, thereby increasing growth and yield of the plant. Provided herein is also a method for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one cell of a plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the stomatal cell is a stomatal progenitor cell. Methods for assessing stomatal conductance and increasing water retention are known to the skilled person. Preferably reduced stomatal conductance and / or reducing stomatal density and / or increased water retention is assessed relative to a reference plant grown under identical conditions, wherein the reference plant has not been subject to modification of its heritable genetic material in order to express a water-forming oxidase in at least one cell of the reference plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the stomatal cell is a stomatal progenitor cell. Stomatal conductance is understood in the art to refer to the rate at which gas exchange of water and CO2occurs through leaf stomata. Conductance may be a function of stomatal aperture, stomatal size and / or stomatal density. Methods for measuring stomatal conductance are well known in the art. For example, stomatal conductance can be determined using an infrared open-gas exchange system. For example, stomatal conductance can be measured using a leaf porometer. For example, stomatal conductance can be measured using thermography-based methods, thermal imaging, and / or infrared temperature sensing. For example, stomatal conductance can also be estimated from sap- flux measurements. For example, stomatal conductance can also be measured at the canopy level using techniques such as multispectral imaging and / or remote sensing. For example, stomatal conductance can also be measured at the canopy level using techniques such as eddy covariance measurements of the latent heat flux. A person skilled in the art will recognise that there are a wide variety of techniques which can be used to measure stomatal conductance at multiple scales (individual leaf, whole plant, canopy etc). Stomatal density is understood in the art to refer to the number of stomata per unit area of a leaf. Stomatal density can refer to either the abaxial or adaxial leaf surface. It well understood that an increase in stomatal density may lead to an increase in stomatal conductance, whereas a decrease in stomatal conductance may lead to a decrease in stomatal conductance. Methods for measuring stomatal density are well known in the art. For example, measuring stomatal density may preferably comprise obtaining epidermal impressions from the abaxial or adaxial surface of plants leaves, visualizing the epidermal impressions under a suitable microscope, and determining stomatal density counts across a plurality of independent fields per leaf. Water retention in the context of the methods of the invention preferably refers to reduction in water loss by transpiration. Increased water retention may therefore be a function of decreased stomatal conductance and / or decreased stomatal density. Preferably any one of the methods described herein may comprise growing the plant in water-deficit conditions. Growing may preferably comprise cultivating the plant in water-deficit conditions. Water-deficit conditions are known to the skilled person and exemplary water-deficit conditions are described herein. In the methods described herein, when a phenotypic effect is for example described as being increased or decreased, it is understood that this preferably refers to an increase or decrease relative to a control unmodified plant grown under the same conditions. The skilled person may modify the heritable genetic material of a plant in any suitable way such that a water-forming oxidase is expressed in at least one mesophyll cell of the plant. For example, the skilled person may use any of the methods for generating transgenic plants described herein, such as any suitable method of transformation described herein. The modification may comprise transforming a C3or C4plant with: i. a polynucleotide according to the invention; or ii. a vector according to the invention; or iii. a polynucleotide comprising a promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase. The promoter element of the polynucleotide of iii. may be any promoter element capable of driving expression of an operatively linked gene which is not limited to a plant cell promoter element. The promoter element may comprise, be derived from, or consist of, any suitable promoter known to the skilled person. The promoter element may otherwise be defined according to the promoter element of the polynucleotide provided herein The plant may be any plant described herein, and is most preferably a C3 or C4plant. The water-forming oxidase may be any water-forming oxidase described herein, but is preferably an NADPH water-forming oxidase, an NADH water-forming oxidase, or a bifunctional NAD(P)H water-forming oxidase. Plant product Provided herein is a plant part, plant tissue, plant organ, plant cell, plant protoplast, embryo, callus culture, pollen grain or seed derived from the plant according to the invention, or derived from a plant produced by the method for increasing growth and yield of a plant described herein, optionally wherein the plant part comprises a nucleic acid sequence corresponding to the water-forming oxidase defined according to the invention. In some instances, the plant, plant part, plant tissue, plant organ, plant cell, plant protoplast, embryo, callus culture, pollen grain or seed is not exclusively obtained by essentially biological processes. Use Provided herein is a a use of a water-forming oxidase for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the use comprises cultivating a plant comprising a nucleotide sequence corresponding to the water-forming oxidase defined according to the invention. Preferably, in the use of the invention described herein, the plant is a transgenic plant that has: (i) reduced stomatal conductance; and / or (ii) reduced stomatal density; and / or (iii) increased water retention, compared to a control unmodified plant grown under the same conditions, preferably wherein the plant is a C3or C4plant, preferably wherein the conditions are water-deficit conditions. The features of the use of the invention may be defined according to any polynucleotide of the invention. The use may further comprise any steps defined according to the methods of the invention described herein. For example, the use may comprise a step of generating a transgenic plant by way of transformation such that the plant expresses the water forming oxidase defined according to the polynucleotide of the invention. Examples The present invention will now be described with reference to specific Examples, which should not be construed as in any way limiting. Example 1: Water-forming NADH or NADPH oxidases from multiple different species can be expressed in plant cells To demonstrate that water-forming NADH or NADPH oxidases from multiple different species can be expressed in plants, the genes from Streptococcus mutans SmNOX [SEQ ID NO: 19], Lactobacillus brevis LbNOX [SEQ ID NO: 15 and SEQ ID NO: 17], were codon optimised for expression in plants [respective nucleotide sequences defined by SEQ ID NO: 18, SEQ ID NO: 14, and SEQ ID NO:16] and cloned into the pICH47742 vector (Weber E et al. 2011 PLoS One. 6(2):e16765). Each water-forming oxidase gene cloned into this vector is thus expressed with a C-terminal GFP [SEQ ID NO: 4 and SEQ ID NO: 5] fusion under the control of the 35S CaMV promoter [SEQ ID NO: 2] (Figure 1A). The vectors were introduced into Arabidopsis thaliana leaf protoplasts using Polyethylene glycol-mediated protoplast transformation. In each case, expression was readily detected using confocal microscopy confirming expression of the introduced transgenes (LbNOX and SmNOX variants, Figure 2). Example 2: Engineered water-forming NADH or NADPH oxidases can be expressed in plant cells To demonstrate that engineered water-forming NADH or NADPH oxidases can be expressed in plants the engineered water-forming NADH or NADPH oxidase from Streptococcus mutans SmNOX [SEQ ID NO: 19] was codon optimised for expression in plants [SEQ ID NO: 18] and cloned into the pICH47742 vector. As above, the gene was expressed as a C-terminal GFP [SEQ ID NO: 4 and SEQ ID NO: 5] fusion under the control of the 35S CaMV promoter [SEQ ID NO: 2] (Figure 1A). The vector was introduced into Arabidopsis thaliana leaf protoplasts using Polyethylene glycol-mediated protoplast transformation. Expression was readily detected using confocal microscopy confirming expression of the introduced transgene (SmNOX variants Figure 2). Example 3: Water-forming NADH or NADPH oxidases can be targeted to different subcellular locations in plant cells To demonstrate that water-forming oxidases can be targeted to different subcellular locations in plant cells, the bifunctional water-forming NAD(P)H oxidase from Streptococcus mutans SmNOX was translationally fused at its N-terminus to several different protein sequences, and at its C-terminus to GFP [SEQ ID NO: 4 and SEQ ID NO: 5] (Figure 1B). These proteins included the chloroplast transit peptide from the oxygen evolving protein 16 gene [SEQ ID NO: 8 and SEQ ID NO: 9]. An alternative chloroplast transit peptide from the oxygen evolving protein 23 gene [SEQ ID NO: 10 and SEQ ID NO: 11]. The rubisco small subunit gene [SEQ ID NO: 6 and SEQ ID NO: 7]. The outer envelope protein 9 gene [SEQ ID NO: 12 and SEQ ID NO: 13]. In each case, expression was readily detected using confocal microscopy confirming expression of the introduced transgenes in the correct location. Specifically, SmNOX fused to the sequence encoding the chloroplast transit peptide from oxygen evolving protein 16 [SEQ ID NO: 36 and SEQ ID NO: 37] or 23 [SEQ ID NO: 38 and SEQ ID NO: 39] (Cp SmNOX Figure 2) or to the rubisco small subunit [SEQ ID NO: 34 and SEQ ID NO: 35] localised to the chloroplast (RbcS-SmNOX Figure 2). SmNOX fused to outer envelope protein 9 [SEQ ID NO: 40 and SEQ ID NO: 41] localised to the chloroplast envelope (CIMS SmNOX, Figure 2). Example 4: Expression of water-forming NADH or NADPH oxidases in plants results in enhanced growth compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on plant growth the Streptococcus mutans bifunctional water-forming NAD(P)H oxidase [SEQ ID NO: 18] was cloned into the pAGM37443 vector (Grützner R et al Plant Communications, 2020, 100135). In this vector the bifunctional water-forming NAD(P)H oxidase gene is expressed under the control of the chlorophyll a / b-binding protein 3 (CAB3) promoter [SEQ ID NO: 1] (Figure 1C). This created a vector that expressed SmNOX in the cytosol of the plant cell and was labelled Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19]. A series of compositional forms were also generated where the SmNOX gene was translationally fused at its N-terminus to a number of different protein sequences (Figure 1D). This set comprised a modified version of the water-forming oxidase that was translationally-fused to the oxygen evolving protein 16 transit peptide (SEQ ID NO: 8 and SEQ ID NO: 9) and targeted to the chloroplast (Cp SmNOX SEQ ID NO: 22 and SEQ ID NO: 23 ), a modified version of the water-forming oxidase that was translationally-fused to the rubisco small subunit (SEQ ID NO: 6 and SEQ ID NO: 7) and targeted to the chloroplast (RbcS-SmNOX SEQ ID NO: 20 and SEQ ID NO: 21), and a modified version of the water-forming oxidase that was translationally-fused to the outer envelope protein 9 (SEQ ID NO: 12 and SEQ ID NO: 13) and targeted to the chloroplast intermembrane space (CIMS SmNOX SEQ ID NO: 26 and SEQ ID NO: 27). Arabidopsis thaliana plants were transformed with these vectors using the floral dip method. Single insertion events were isolated and the growth rate, biomass accumulation, plant height, bolting time, and flowering time of the transgenic plants was analysed and compared to non-modified control plants. Plants were grown for 20 days and growth rates of the transgenic plants between day 10 and day 20 were compared to the non-modified control plants. This revealed that all plant lines expressing water-forming oxidases grew faster than non-modified control plants (Figure 3A). Specifically, plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] grew fastest and grew 100% faster than non-modified control plants (p < 0.001, one-way ANOVA). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] grew 80% faster than non-modified control plants (p < 0.001, one-way ANOVA). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] also grew 80% faster than non-modified control plants (p < 0.001, one-way ANOVA). Plants expressing RbcS-SmNOX [SEQ ID NO: 20 and SEQ ID NO: 21] grew 20% faster than non-modified control plants (p < 0.05, one-way ANOVA). Example 5: Expression of water-forming NADH or NADPH oxidases in plants results in enhanced biomass compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on plant biomass accumulation the transgenic plants above were grown in identical conditions and the total rosette area of each plant was measured on day 20. Consistent with the growth rate data above, plants that were expressing water-forming oxidases accumulated more biomass than non-modified control plants over the same period of time (Figure 3B). Specifically, plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] produced a 100% larger leaf area than control plants (p < 0.001, one-way ANOVA). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] produced an 80% larger leaf area than control plants (p < 0.001, one-way ANOVA). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] produced an 80% larger leaf area than control plants (p < 0.001, one-way ANOVA). Plants expressing RbcS-SmNOX [SEQ ID NO: 20 and SEQ ID NO: 21] produced a 20% larger leaf area than control plants (p < 0.05, one-way ANOVA). Example 6: Expression of water-forming NADH or NADPH oxidases in plants results in enhanced inflorescence size compared to unmodified plants To provide an additional demonstration of the impact of expression of water- forming oxidases on plant yield the transgenic plants above were grown in identical conditions and the height of the inflorescence of each plant was measured on day 32. Consistent with the growth rate and biomass data above, plants that were expressing water- forming oxidases produced larger inflorescences than non-modified control plants over the same period of time (Figure 3C). Specifically, plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] produced a 20% taller primary inflorescence than control plants (p < 0.001, one-way ANOVA). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] produced a 15% taller primary inflorescence than control plants (p < 0.001, one-way ANOVA). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] produced a 14% taller primary inflorescence than control plants (p < 0.001, one-way ANOVA). Plants expressing RbcS-SmNOX [SEQ ID NO: 20 and SEQ ID NO: 21] produced a primary inflorescence that was not significantly different to control plants (p > 0.05, one-way ANOVA). Example 7: Expression of water-forming NADH or NADPH oxidases in plants results in a reduction in flowering time compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on an additional plant yield component the transgenic plants above were grown in identical conditions and the time it took for each plant to flower was recorded. Consistent with the growth rate, biomass accumulation, and primary inflorescence size data above, plants that were expressing water-forming oxidases flowered earlier than non-modified control plants (Figure 3D). Specifically, plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] flowered on average 1.3 days earlier than non-modified control plants p < 0.001, one-way ANOVA). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] flowered on average 0.9 days earlier than non-modified control plants p < 0.001, one-way ANOVA). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] flowered on average 0.8 days earlier than non-modified control plants p < 0.01, one-way ANOVA). Plants expressing RbcS-SmNOX [SEQ ID NO: 20 and SEQ ID NO: 21] flowered on average at the same time as non-modified control plants (p > 0.05 , one-way ANOVA). Example 8: Expression of water-forming NADH or NADPH oxidases in plants results in a reduction in stomatal density compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on plant stomatal development, the transgenic plants above were grown in identical conditions and stomatal density was measured from the epidermal impressions of the leaf abaxial surface. Leaves from plants that were expressing water-forming oxidases exhibited lower stomatal density compared to non-modified control plants of the same age (Figure 4A). Specifically, plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] exhibited 30.6% lower stomatal density than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] exhibited 22.8% lower stomatal density than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] exhibited 20.5% lower stomatal density than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Example 9: Expression of water-forming NADH or NADPH oxidases in plants results in a reduction in stomatal conductance compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on leaf gas exchange, the transgenic plants above were grown in identical conditions and the light- saturated rate of stomatal conductance was measured. Consistent with the reduction in stomatal density, plants that were expressing water-forming oxidases exhibited a reduced stomatal conductance compared to non-modified control plants (Figure 4B). Specifically, plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] exhibited a 27.4% lower stomatal conductance than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] exhibited a 24.5% lower stomatal conductance than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] exhibited a 22.5% lower stomatal conductance than control plants (p < 0.001, Two-way ANOVA and Fisher LSD post-hoc analysis). Example 10: Expression of water-forming NADH or NADPH oxidases in plants results in an enhancement of photosynthetic water-use efficiency compared to unmodified plants To demonstrate the impact of the expression of water-forming oxidases on plant photosynthetic water-use efficiency, the transgenic plants above were grown in identical conditions and the light-saturated intrinsic photosynthetic water-use efficiency was measured as the ratio of photosynthetic CO2assimilation to stomatal gaseous conductance to water vapour. Plants that were expressing water-forming oxidases exhibited an enhanced photosynthetic water-use efficiency compared to non-modified control plants (Figure 4C). Specifically, plants expressing Cp SmNOX [SEQ ID NO: 22 and SEQ ID NO: 23] exhibited a 17.6% increase in photosynthetic water-use efficiency compared to control plants (p < 0.05, Two-way ANOVA and Fisher LSD post-hoc analysis). Plants expressing CIMS SmNOX [SEQ ID NO: 26 and SEQ ID NO: 27] exhibited a 16.8% increase in photosynthetic water-use efficiency compared to control plants (p < 0.05, Two- way ANOVA and Fisher LSD post-hoc analysis). Plants expressing Cytosolic SmNOX [SEQ ID NO: 18 and SEQ ID NO: 19] exhibited a 12.6% increase in photosynthetic water- use efficiency compared to control plants (p < 0.05, Two-way ANOVA and Fisher LSD post-hoc analysis).

Claims

CLAIMS 1. A polynucleotide comprising a plant cell promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase.

2. The polynucleotide according to claim 1, wherein the plant cell promoter element comprises, is derived from, or consists of, the promoter of a gene expressed in photosynthetic cells, preferably specifically expressed in mesophyll cells and / or is a C3or C4plant cell promoter.

3. The polynucleotide according to claim 1 or claim 2, wherein the plant cell promoter element is: a. derived from, or consists of, a promoter from a cell capable of photosynthesis, preferably wherein the cell is a mesophyll; or b. derived from, or consists of, one of the following gene promoters: rubisco small subunit (pRBCS1A), chlorophyll a / b-binding protein (cab), and more preferably the CAB3 promoter, PEPC, IQD22, AT1G70958, SQE6, XTH6, PAL1, CORI3, YAB3, LHCB2.4, CRR23, SPS4F, ENH1, or COR414- TM1; or c. derived from, or consists of, a promoter of a gene expressed, or specifically expressed, in a cell of a plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the cell is a stomatal progenitor cell.

4. The polynucleotide according to any one of claims 1 to 3, wherein the promoter is inducible or ubiquitously active.

5. The polynucleotide according to any one of claims 1 to 4, wherein the sequence encoding the water-forming oxidase is codon optimised for expression in a plant, preferably wherein the plant is a C3 or C4plant.

6. The polynucleotide according to any one of claims 1 to 5, wherein the water- forming oxidase is an NADPH water-forming oxidase, an NADH water-forming oxidase, or a bifunctional NAD(P)H water-forming oxidase.

7. The polynucleotide according to claim 6, wherein the NADPH water-forming oxidase or NADH water-forming oxidase is derived from bacteria.

8. The polynucleotide according to claim 6 or claim 7, wherein the sequence encoding the NADPH water-forming oxidase or the NADH water-forming oxidase comprises or consists of the sequence according to SEQ ID NO: 14, and / or SEQ ID NO: 16, and / or SEQ ID NO: 18, or an active variant thereof.

9. The polynucleotide according to claim 8, wherein the active variant is characterised as comprising a sequence sharing at least 50% sequence identity to SEQ ID NO: 14, or SEQ ID NO: 16, or SEQ ID NO: 18, or at least 55%, at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97% or at least 99% sequence identity to SEQ ID NO: 14, or SEQ ID NO: 16, or SEQ ID NO:

18.

10. The polynucleotide according to any one of claims 1 to 9, wherein the polynucleotide further comprises a terminator.

11. The polynucleotide according to any one of claims 1 to 10, wherein the nucleotide sequence further encodes one or more of: i. a protein that differs from the water-forming oxidase; ii. a target peptide; and iii. a transmembrane domain, optionally wherein the one or more of i. to iii. are separated from the water-forming oxidase by a linker.

12. A vector comprising the polynucleotide according to any one of claims 1 to 11.

13. The vector according to claim 12, wherein the vector comprises an origin of replication, and a T-DNA right border repeat of a Ti or Ri plasmid, optionally further comprising a left border repeat of a Ti or Ri plasmid, and at least one bacterial selectable marker.

14. The vector according to claim 12 of claim 13, wherein the vector further comprises one or more of: i. an enhancer; ii. a plant selectable marker; iii. a multicloning site; and iv. a recombination site.

15. A composition for transforming plant cells, the composition comprising a polynucleotide according to any one of claim 1 to 11 and / or a vector according to any one of claims 12 to 14, preferably wherein the composition comprises a microparticle complexed with the polynucleotide and or the vector.

16. A cell comprising the polynucleotide according to any one of claims 1 to 11, or comprising the vector according to any one of claims 12 to 14.

17. The cell according to claim 16, wherein the cell is a bacterial cell, preferably wherein the bacterial cell is an E. coli cell, an Agrobacterium sp. cell or preferably an A. tumefaciens cell.

18. The cell according to claim 16, wherein the cell is a C3plant cell or a C4plant cell, preferably wherein the cell is a cell of a plant leaf epidermis and / or is capable ofundertaking photosynthesis, preferably wherein the cell is a stomatal cell, and more preferably wherein the cell is a stomatal progenitor cell.

19. A plant or part thereof comprising: i. a cell according to claim 18; or ii. a cell comprising a polynucleotide which comprises a promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase.

20. The plant according to claim 19, wherein the plant is a transgenic plant that has enhanced growth compared to a control unmodified plant grown under the same conditions, preferably wherein the plant is a C3or C4plant, preferably wherein the conditions are water-deficit conditions.

21. The plant according to claim 19 or claim 20, wherein the plant is a C3 plant selected from Soy (Glycine max), cotton (Gossypium hirsutum), oilseed rape / Cannola (B. napus subsp. Napus), potato (Solanum tuberosum), tomato (Solanum lycopersicum), wheat (Triticum aestivum), barley (Hordeum vulgare), oat (Avena sativa), rice (Oryza sativa), rye (Secale cereal), pigeon pea (Cajanus cajan), cowpea (Vigna unguiculata), pea (Pisum sativum), sugar beet (Beta vulgaris), cassava (Manihot esculenta), sweet potato (Ipomoea batatas), yam (Dioscorea spp.), peanut (Arachis hypogaea), Sunflower (Helianthus annuus), flax (Linum spp.), beans (Phaseolus vulgaris), lima bean (Phaseolus lunatus), mung bean (Phaseolus mung), Adzuki bean (Phaseolus angularis), chickpea (Cicer arietinum), buckwheat (Fagopyrum esculentum), tobacco (Nicotiana tabacum), cannabis (Cannabis sativa), oil palm (Elaeis guineensis), Sycamore (Acer pseudoplatanus), Sweet chestnut (Castanea sativa), Poplar (Populus spp.), Eucalyptus (Sucalyptus spp.), Plantain / banana (Musa acuminate), or rubber (Hevea brasiliensis) plant, or wherein the plant is a C4plant selected from maize (Zea mays), sorghm (Sorghm bicolor), sugar cane, millet or teff.

22. A method for increasing photosynthetic capacity of a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one mesophyll cell of the plant, thereby increasing photosynthetic capacity of the plant.

23. A method for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the plant is a C3or C4plant, the method comprising modifying the heritable genetic material of the plant such that a water-forming oxidase is expressed in at least one cell of a plant leaf epidermis, preferably wherein the cell is a stomatal cell, and more preferably wherein the cell is a stomatal progenitor cell.

24. The method according to claim 22 or claim 23, wherein the water-forming oxidase is an NADPH water-forming oxidase, an NADH water-forming oxidase, or a bifunctional NAD(P)H water-forming oxidase.

25. The method according to any one of claims 22 to 24, wherein the modifying comprises transforming a plant with: i. a polynucleotide according to any one of claims 1 to 11; or ii. a vector according to any one of claims 12 to 14; or iii. a polynucleotide comprising a promoter element operatively linked to a nucleotide sequence that encodes a water-forming oxidase.

26. The method according to any one of claims 22 to 25, wherein the method comprises growing the plant in water-deficit conditions.

27. A plant part, plant tissue, plant organ, plant cell, plant protoplast, embryo, callus culture, pollen grain or seed derived from the plant according to any one of claims 19 to 21, or derived from a plant produced by the method according to any one of claims 22 to 26, optionally wherein the plant part comprises a nucleotide sequence corresponding to the water-forming oxidase defined according to claims 1 to 11.

28. A use of a water-forming oxidase for: (i) reducing stomatal density of a plant; and / or (ii) reducing stomatal conductance of a plant; and / or (iii) increasing water retention in a plant, preferably wherein the use comprises cultivating a plant comprising a nucleotide sequence corresponding to the water-forming oxidase defined according to claims 1 to 11.

29. The use according to claim 28, wherein the plant is a transgenic plant that has: (i) reduced stomatal density; and / or (ii) reduced stomatal conductance; and / or (iii) increased water retention, compared to a control unmodified plant grown under the same conditions, preferably wherein the plant is a C3or C4plant, preferably wherein the conditions are water-deficit conditions.

Images