Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction

Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO<sub>2</sub> 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...

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Main Authors: Thibault Fogeron, Yun Li, Marc Fontecave
Format: Article
Language:English
Published: MDPI AG 2022-09-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/27/18/5989
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author Thibault Fogeron
Yun Li
Marc Fontecave
author_facet Thibault Fogeron
Yun Li
Marc Fontecave
author_sort Thibault Fogeron
collection DOAJ
description Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO<sub>2</sub> 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 CO<sub>2</sub> reduction are less studied compared to the oxygen atom transfer (OAT) reaction. Herein, we present recent results of structural and functional models of FDH.
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spelling doaj.art-beb618b311434abf95e270903d8f38d92023-11-23T18:02:23ZengMDPI AGMolecules1420-30492022-09-012718598910.3390/molecules27185989Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide ReductionThibault Fogeron0Yun Li1Marc Fontecave2Laboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Paris Sorbonne University, 11 Place Marcelin Berthelot, CEDEX 05, 75231 Paris, FranceLaboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Paris Sorbonne University, 11 Place Marcelin Berthelot, CEDEX 05, 75231 Paris, FranceLaboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Paris Sorbonne University, 11 Place Marcelin Berthelot, CEDEX 05, 75231 Paris, FranceFormate dehydrogenases (FDH) reversibly catalyze the interconversion of CO<sub>2</sub> 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 CO<sub>2</sub> reduction are less studied compared to the oxygen atom transfer (OAT) reaction. Herein, we present recent results of structural and functional models of FDH.https://www.mdpi.com/1420-3049/27/18/5989formate dehydrogenasesstructural modelsfunctional modelsdithiolene complexescarbon dioxide reduction
spellingShingle Thibault Fogeron
Yun Li
Marc Fontecave
Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
Molecules
formate dehydrogenases
structural models
functional models
dithiolene complexes
carbon dioxide reduction
title Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
title_full Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
title_fullStr Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
title_full_unstemmed Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
title_short Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction
title_sort formate dehydrogenase mimics as catalysts for carbon dioxide reduction
topic formate dehydrogenases
structural models
functional models
dithiolene complexes
carbon dioxide reduction
url https://www.mdpi.com/1420-3049/27/18/5989
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AT marcfontecave formatedehydrogenasemimicsascatalystsforcarbondioxidereduction