Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.


Journal

Dalton transactions (Cambridge, England : 2003)
ISSN: 1477-9234
Titre abrégé: Dalton Trans
Pays: England
ID NLM: 101176026

Informations de publication

Date de publication:
21 Sep 2021
Historique:
entrez: 21 9 2021
pubmed: 22 9 2021
medline: 22 9 2021
Statut: epublish

Résumé

Elucidating the distribution of intermediates at the active site of redox metalloenzymes is vital to understanding their highly efficient catalysis. Here we demonstrate that it is possible to generate, and detect, the key catalytic redox states of an [FeFe]-hydrogenase in a protein crystal. Individual crystals of the prototypical [FeFe]-hydrogenase I from

Identifiants

pubmed: 34545877
doi: 10.1039/d1dt02219a
pmc: PMC8453692
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

12655-12663

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Auteurs

Simone Morra (S)

Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.

Jifu Duan (J)

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

Martin Winkler (M)

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

Philip A Ash (PA)

Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.

Thomas Happe (T)

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

Kylie A Vincent (KA)

Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, United Kingdom. kylie.vincent@chem.ox.ac.uk.

Classifications MeSH