Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction

Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO(2) 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...

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Detalles Bibliográficos
Autores principales: Fogeron, Thibault, Li, Yun, Fontecave, Marc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9506188/
https://www.ncbi.nlm.nih.gov/pubmed/36144724
http://dx.doi.org/10.3390/molecules27185989
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author Fogeron, Thibault
Li, Yun
Fontecave, Marc
author_facet Fogeron, Thibault
Li, Yun
Fontecave, Marc
author_sort Fogeron, Thibault
collection PubMed
description Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO(2) 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(2) 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 pubmed-95061882022-09-24 Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction Fogeron, Thibault Li, Yun Fontecave, Marc Molecules Review Formate dehydrogenases (FDH) reversibly catalyze the interconversion of CO(2) 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(2) reduction are less studied compared to the oxygen atom transfer (OAT) reaction. Herein, we present recent results of structural and functional models of FDH. MDPI 2022-09-14 /pmc/articles/PMC9506188/ /pubmed/36144724 http://dx.doi.org/10.3390/molecules27185989 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Fogeron, Thibault
Li, Yun
Fontecave, Marc
Formate Dehydrogenase Mimics as Catalysts for 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 Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9506188/
https://www.ncbi.nlm.nih.gov/pubmed/36144724
http://dx.doi.org/10.3390/molecules27185989
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AT liyun formatedehydrogenasemimicsascatalystsforcarbondioxidereduction
AT fontecavemarc formatedehydrogenasemimicsascatalystsforcarbondioxidereduction

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