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

Ami Kobayashi, Midori Taketa, Keisei Sowa, Kenji Kano, Yoshiki Higuchi, Hideaki Ogata

Journal: IUCrJ 2023;10(Pt 5):544-554

PMID: 37668215

Free Full Text on PubMed Central View on PubMed

Abstract

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.

open access.

Address: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan.; Graduate School of Science, University of Hyogo, Koto 3-2-1 Kamigori, Ako, Hyogo 678-1297, Japan.; Office of Society Academia Collaboration for Innovation, Kyoto University, Gokasho, Uji 611-0011, Japan.

DOI: 10.1107/S2052252523006437

Link outs

Free resources

Full Text Sources:

Subscription / membership required

Full Text Sources:

http://scripts.iucr.org/cgi-bin/paper?S20522525230...

MeSH Terms: Biotechnology, Carbon Dioxide, Catalysis, Electrons, Formate Dehydrogenases