A Conserved Binding Pocket in HydF is Essential for Biological Assembly and Coordination of the Diiron Site of [FeFe]-Hydrogenases.

Journal

Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056

Informations de publication

Date de publication:
31 May 2024
Historique:
medline: 31 5 2024
pubmed: 31 5 2024
entrez: 31 5 2024
Statut: aheadofprint

Résumé

The active site cofactor of [FeFe]-hydrogenases consists of a cubane [4Fe-4S]-cluster and a unique [2Fe-2S]-cluster, harboring unusual CO- and CN

Identifiants

DOI: 10.1021/jacs.4c01635 PMID: 38819401
pubmed: 38819401
doi: 10.1021/jacs.4c01635
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Rieke Haas (R)

Photobiotechnology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany.
ORCID: 0000-0002-3023-9798

Oliver Lampret (O)

Photobiotechnology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany.

Shanika Yadav (S)

Inorganic Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801 Bochum, Germany.
ORCID: 0000-0003-1155-2241

Ulf-Peter Apfel (UP)

Inorganic Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801 Bochum, Germany.
ORCID: 0000-0002-1577-2420

Thomas Happe (T)

Photobiotechnology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany.
ORCID: 0000-0003-1206-5234

Classifications MeSH