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 o...

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Published inIUCrJ Vol. 10; no. 5; pp. 544 - 554
Main Authors Kobayashi, Ami, Taketa, Midori, Sowa, Keisei, Kano, Kenji, Higuchi, Yoshiki, Ogata, Hideaki
Format Journal Article
LanguageEnglish
Published England International Union of Crystallography 01.09.2023
Subjects
biotechnological applications
Biotechnology
Carbon Dioxide
Catalysis
Electrons
formate dehydrogenases
Formate Dehydrogenases - genetics
methylorubrum extorquens am1
mo/w enzymes
Mo/W enzymes
Methylorubrum extorquens AM1
biotechnological applications
formate dehydrogenases
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ISSN2052-2525
2052-2525
DOI10.1107/S2052252523006437

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Summary: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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ISSN:2052-2525
2052-2525
DOI:10.1107/S2052252523006437