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4 results about "Ferredoxin" patented technology

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

Recombinant saccharomyces cerevisiae as well as construction method and application thereof

The invention relates to the field of astaxanthin synthesis, and discloses recombinant saccharomyces cerevisiae as well as a construction method and application thereof. The recombinant saccharomyces cerevisiae provided by the invention comprises the following exogenous genes: coding genes of beta-carotene hydroxylase CrtZ, beta-carotene ketolase CrtW, nicotinamide adenine dinucleotide kinase, ferredoxin-NADPH (nicotinamide adenine dinucleotide phosphate) oxidoreductase and ferredoxin; on the basis of the gene, other related genes are further introduced to realize that CrtZ and CrtW are positioned in lipid droplets by lipid droplet targeting peptide Olesion, so that the yield of astaxanthin is increased, finally geranyl-geranyl diphosphate synthase, phytoene dehydrogenase and phytoene synthase are targeted to endoplasmic reticulum through endoplasmic reticulum targeting peptide, and the yield of astaxanthin is increased. Therefore, the yield of the fermentation tank is up to 440mg / L. The recombinant saccharomyces cerevisiae provided by the invention is clear in genetic background, can stably and efficiently produce astaxanthin, and has a wide application prospect.
Owner:YIXING INST OF FOOD & BIOTECHNOLOGY CO LTD +1

Compounds for targeting ferredoxin 2 (FDX2) in friedreich ataxia (FRDA)

PCT designated stageWO2026107101A2Organic active ingredientsDNA/RNA fragmentationDisease patientFrataxin
Described herein are compositions and methods for treating subjects with disorders associated with mutations in the FXN gene and / or that have reduced expression of frataxin protein, e.g., Friedreich ataxia (FRDA), using inhibitors of ferredoxin 2 (FDX2) that decreases FDX2 protein expression.
Owner:THE GENERAL HOSPITAL CORP +1

Method for producing phycocyanobilin using a recombinant Escherichia coli

Disclosed is a method for producing phycocyanobilin by use of a recombinant Escherichia coli that express heterologous heme oxygenase ho1 and ferredoxin oxidoreductase pcyA derived from Synechocystis sp. PCC6803. According to the present disclosure, heterologous expression of ho1 and pcyA genes leads to conversion of heme to an intermediate biliverdin for phycocyanobilin synthesis, and reduces the accumulation of biliverdin in the process of the phycocyanobilin synthesis. The genome of E. coli is further engineered to overexpress related genes of a metabolic pathway of phycocyanobilin, and a strain of recombinant E. coli with high yield of phycocyanobilin is obtained. The recombinant E. coli strain is cultured for 36 hr in a system using glycerol as a substrate, and the phycocyanobilin yield can reach 147 mg / L.
Owner:JIANGNAN UNIV

Method for synthesizing p-hydroxybenzaldehyde from p-hydroxybenzoic acid through light-driven enzyme catalysis

The invention provides a method for synthesizing p-hydroxybenzaldehyde from p-hydroxybenzoic acid through light-driven enzyme catalysis. A used reaction system comprises carboxylic acid reductase (CAR), a photosynthesis unit, ferredoxin (Fdx) and phosphotransferase (PAP). According to the method, light energy is utilized to drive spinach capsule membranes to co-regenerate NADPH and ATP, and the problem that carboxylic acid reductase needs coenzyme supply of NADPH and ATP at the same time is solved. According to the method, a light energy driven enzyme catalysis method is adopted, a biological photosynthetic reaction is used for replacing a traditional high-energy-consumption and high-pollution chemical process, and green and efficient synthesis of p-hydroxybenzaldehyde is achieved through cooperation of double-coenzyme light regeneration and enzyme specific catalysis.
Owner:TIANJIN INST OF IND BIOTECH CHINESE ACADEMY OF SCI