Nitric oxide reductase analogs and preparation method thereof

Abstract

The invention discloses nitric oxide reductase analogs and a preparation method thereof. Chemical names of the analogs comprise ferriporphyrin NO complexes and ferriporphyrin chlorides, bound ferriporphyrin NO complexes comprising C2-C5 alkyl are 1-FeNO to 4-FeNO, and corresponding precursor compounds, i.e., ferriporphyrin chlorides are 1-FeCl to 4-FeCl. The preparation method comprises the stepsof applying alkyl bridged bis(5-tert-butyl salicylaldehyde), synthesizing the ferriporphyrin chlorides by using a metal template method, carrying out decomposition by using nitrous acid to produce NO,and subjecting the NO to axial substitution, thereby obtaining the ferriporphyrin NO complexes. According to the method, by using the characteristic that a metal electron structure is regulated and controlled through porphyrin ring deformation, the interconversion of axial NO ligands to nucleophilic from electrophilic is achieved. The analogs are of nonplanar-structure continuous variation whichare similar to variation of structures and functions of nitric oxide reductase, the synthesis steps are few, the raw materials are economical and readily available, separation and purification costs are relatively low, and thus, the analogs are relatively ideal analogs of the nitric oxide reductase.

Description

technical field [0001] The invention relates to chemical biology and biomimetic synthesis, in particular to a type of nitric oxide reductase mimetic and a preparation method thereof, which can be used for the research of NO physiological function and physiological mechanism. Background technique [0002] Nitric oxide (NO), an important signaling molecule in cardiovascular, immune and cancer, has shown some unexpected roles and was once named "Molecule of the Year" by Science. Nitric oxide reductase (NOR) is a class of enzymes that control the balance and conversion of NO in vivo, but it is very difficult to reproduce and simulate the structure and function of this reductase in vitro. NOR exists in hemoglobin and is a kind of iron porphyrin NO complex, which is a homologous protease with heme, and its function largely depends on the twist of the porphyrin ring. Numerous recent mechanistic studies have also shown that the catalytic performance of NOR is related to the dynamic...

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Problems solved by technology

[0003] The content of natural NOR in organisms is extremely low, and its function cannot be separated from the innate physiological environment. However, there is currently no artificial material that can match the structure and function of natural NOR for corresponding structure-performance correlation simulations. Research

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