Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle.


Journal

Science advances
ISSN: 2375-2548
Titre abrégé: Sci Adv
Pays: United States
ID NLM: 101653440

Informations de publication

Date de publication:
05 2021
Historique:
received: 06 01 2021
accepted: 14 04 2021
entrez: 29 5 2021
pubmed: 30 5 2021
medline: 30 5 2021
Statut: epublish

Résumé

Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C

Identifiants

pubmed: 34049880
pii: 7/22/eabg4474
doi: 10.1126/sciadv.abg4474
pmc: PMC8163085
pii:
doi:

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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Auteurs

Michael Rohde (M)

Institute for Biochemistry, University of Freiburg, Albertstrasse 21, 79104 Freiburg, Germany.

Konstantin Laun (K)

Institute of Chemistry, Technical University of Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.

Ingo Zebger (I)

Institute of Chemistry, Technical University of Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.

Sven T Stripp (ST)

Institute of Experimental Physics, Department of Physics, Free University of Berlin, Arnimallee 14, 14195 Berlin, Germany.

Oliver Einsle (O)

Institute for Biochemistry, University of Freiburg, Albertstrasse 21, 79104 Freiburg, Germany. einsle@biochemie.uni-freiburg.de.

Classifications MeSH