Establishing a Thermodynamic Landscape for the Active Site of Mo-Dependent Nitrogenase.
Biosensing Techniques
Catalysis
Catalytic Domain
Coenzymes
Electrochemical Techniques
/ instrumentation
Electrolysis
Electron Transport
Enzymes, Immobilized
/ chemistry
Hydrogels
/ chemistry
Magnetic Resonance Spectroscopy
Molybdenum
/ metabolism
Molybdoferredoxin
/ chemistry
Nitrogen
/ chemistry
Nitrogenase
/ chemistry
Oxidoreductases
/ chemistry
Polyethyleneimine
/ chemistry
Thermodynamics
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:
30 10 2019
30 10 2019
Historique:
pubmed:
3
10
2019
medline:
5
11
2020
entrez:
3
10
2019
Statut:
ppublish
Résumé
Nitrogenase enzymes are the only biological catalysts able to convert N
Identifiants
pubmed: 31577428
doi: 10.1021/jacs.9b06546
doi:
Substances chimiques
Coenzymes
0
Enzymes, Immobilized
0
Hydrogels
0
Molybdoferredoxin
0
Molybdenum
81AH48963U
Polyethyleneimine
9002-98-6
Oxidoreductases
EC 1.-
Nitrogenase
EC 1.18.6.1
nitrogenase reductase
EC 1.18.6.1
Nitrogen
N762921K75
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
17150-17157Commentaires et corrections
Type : ErratumIn