Structural Enzymology of Nitrogenase Enzymes.
Journal
Chemical reviews
ISSN: 1520-6890
Titre abrégé: Chem Rev
Pays: United States
ID NLM: 2985134R
Informations de publication
Date de publication:
24 06 2020
24 06 2020
Historique:
pubmed:
17
6
2020
medline:
8
6
2021
entrez:
16
6
2020
Statut:
ppublish
Résumé
The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving two component proteins, MgATP and reductant. At center stage of this process resides the active site cofactor, a complex metallocluster organized around a trigonal prismatic arrangement of iron sites surrounding an interstitial carbon. As a consequence of the choreography, electrons and protons are delivered to the active site for transfer to the bound N
Identifiants
pubmed: 32538623
doi: 10.1021/acs.chemrev.0c00067
pmc: PMC8606229
mid: NIHMS1754447
doi:
Substances chimiques
Metals, Heavy
0
Ammonia
7664-41-7
Nitrogenase
EC 1.18.6.1
Nitrogen
N762921K75
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
4969-5004Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM045162
Pays : United States
Organisme : NIGMS NIH HHS
ID : R37 GM045162
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
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