Structure and function relationship of formate de­hydrogenases: an overview of recent progress

Formate de­hydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily...

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Autores principales: Kobayashi, Ami, Taketa, Midori, Sowa, Keisei, Kano, Kenji, Higuchi, Yoshiki, Ogata, Hideaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2023
Materias:
Topical Reviews
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10478512/
https://www.ncbi.nlm.nih.gov/pubmed/37668215
http://dx.doi.org/10.1107/S2052252523006437
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author Kobayashi, Ami
Taketa, Midori
Sowa, Keisei
Kano, Kenji
Higuchi, Yoshiki
Ogata, Hideaki
author_facet Kobayashi, Ami
Taketa, Midori
Sowa, Keisei
Kano, Kenji
Higuchi, Yoshiki
Ogata, Hideaki
author_sort Kobayashi, Ami
collection PubMed
description Formate de­hydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the di­methyl­sulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized.
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spelling pubmed-104785122023-09-06 Structure and function relationship of formate de­hydrogenases: an overview of recent progress Kobayashi, Ami Taketa, Midori Sowa, Keisei Kano, Kenji Higuchi, Yoshiki Ogata, Hideaki IUCrJ Topical Reviews Formate de­hydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the di­methyl­sulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized. International Union of Crystallography 2023-09-01 /pmc/articles/PMC10478512/ /pubmed/37668215 http://dx.doi.org/10.1107/S2052252523006437 Text en © Ami Kobayashi et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Topical Reviews
Kobayashi, Ami
Taketa, Midori
Sowa, Keisei
Kano, Kenji
Higuchi, Yoshiki
Ogata, Hideaki
Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title_full Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title_fullStr Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title_full_unstemmed Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title_short Structure and function relationship of formate de­hydrogenases: an overview of recent progress
title_sort structure and function relationship of formate de­hydrogenases: an overview of recent progress
topic Topical Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10478512/
https://www.ncbi.nlm.nih.gov/pubmed/37668215
http://dx.doi.org/10.1107/S2052252523006437
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