Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State.
Algal Proteins
/ antagonists & inhibitors
Bacterial Proteins
/ antagonists & inhibitors
Carbon Isotopes
/ chemistry
Carbon Monoxide
/ chemistry
Catalytic Domain
Chlamydomonas reinhardtii
/ enzymology
Clostridium
/ enzymology
Coordination Complexes
/ chemistry
Density Functional Theory
Electron Spin Resonance Spectroscopy
Enzyme Inhibitors
/ chemistry
Hydrogenase
/ antagonists & inhibitors
Iron
/ chemistry
Iron-Sulfur Proteins
/ antagonists & inhibitors
Ligands
Models, Chemical
Molecular Structure
Journal
The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034
Informations de publication
Date de publication:
18 Jun 2020
18 Jun 2020
Historique:
pubmed:
19
5
2020
medline:
9
2
2021
entrez:
19
5
2020
Statut:
ppublish
Résumé
The active site of [FeFe] hydrogenase features a binuclear iron cofactor Fe
Identifiants
pubmed: 32420744
doi: 10.1021/acs.jpclett.0c01352
pmc: PMC7309315
doi:
Substances chimiques
Algal Proteins
0
Bacterial Proteins
0
Carbon Isotopes
0
Coordination Complexes
0
Enzyme Inhibitors
0
Iron-Sulfur Proteins
0
Ligands
0
Carbon Monoxide
7U1EE4V452
Iron
E1UOL152H7
iron hydrogenase
EC 1.12.-
Hydrogenase
EC 1.12.7.2
Carbon-13
FDJ0A8596D
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4597-4602Références
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