Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction

被引：7

作者：

Fogeron, Thibault ^{[1
,2
]}

Li, Yun ^{[1
]}

Fontecave, Marc ^{[1
]}

机构：

[1] Paris Sorbonne Univ, Coll France, Lab Chim Proc Biol, UMR 8229 CNRS, 11 Pl Marcelin Berthelot, F-75231 Paris 05, France

[2] Univ Lyon, Ecole Normale Super Lyon, Lab Chim, CNRS UMR 5182, 46 Allee dItalie, F-69364 Lyon, France

来源：

MOLECULES | 2022年 / 27卷 / 18期

关键词：

formate dehydrogenases; structural models; functional models; dithiolene complexes; carbon dioxide reduction; CRYSTAL-STRUCTURE; ELECTROCATALYTIC REDUCTION; ACTIVE-SITES; MOLYBDENUM COFACTOR; HYDROGEN EVOLUTION; ANALOGS RELEVANT; CO2; REDUCTION; COMPLEXES; TUNGSTEN; DITHIOLENE;

D O I：

10.3390/molecules27185989

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO2 to formate. They belong to the family of molybdenum and tungsten-dependent oxidoreductases. For several decades, scientists have been synthesizing structural and functional model complexes inspired by these enzymes. These studies not only allow for finding certain efficient catalysts but also in some cases to better understand the functioning of the enzymes. However, FDH models for catalytic CO2 reduction are less studied compared to the oxygen atom transfer (OAT) reaction. Herein, we present recent results of structural and functional models of FDH.

引用

页数：19

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