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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MDPI AG
2022-09-01
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Series: | Molecules |
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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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format | Article |
id | doaj.art-beb618b311434abf95e270903d8f38d9 |
institution | Directory Open Access Journal |
issn | 1420-3049 |
language | English |
last_indexed | 2024-03-09T23:01:23Z |
publishDate | 2022-09-01 |
publisher | MDPI AG |
record_format | Article |
series | Molecules |
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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