Stability of the H-cluster under whole-cell conditions-formation of an H
Biophysics
Electron paramagnetic resonance (EPR)
Enzyme mechanism
Hydrogenase
Metalloenzymes
Journal
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
ISSN: 1432-1327
Titre abrégé: J Biol Inorg Chem
Pays: Germany
ID NLM: 9616326
Informations de publication
Date de publication:
04 2022
04 2022
Historique:
received:
20
09
2021
accepted:
03
01
2022
pubmed:
9
3
2022
medline:
12
4
2022
entrez:
8
3
2022
Statut:
ppublish
Résumé
Hydrogenases are metalloenzymes that catalyze the reversible oxidation of molecular hydrogen into protons and electrons. For this purpose, [FeFe]-hydrogenases utilize a hexanuclear iron cofactor, the H-cluster. This biologically unique cofactor provides the enzyme with outstanding catalytic activities, but it is also highly oxygen sensitive. Under in vitro conditions, oxygen stable forms of the H-cluster denoted H
Identifiants
pubmed: 35258679
doi: 10.1007/s00775-022-01928-5
pii: 10.1007/s00775-022-01928-5
pmc: PMC8960641
doi:
Substances chimiques
Iron-Sulfur Proteins
0
Protons
0
Sulfides
0
Hydrogen
7YNJ3PO35Z
Hydrogenase
EC 1.12.7.2
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
345-355Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : SPP1927
Organisme : H2020 European Research Council
ID : 714102
Organisme : H2020 European Research Council
ID : 819580
Organisme : FP7 Ideas: European Research Council
ID : 765376
Informations de copyright
© 2022. The Author(s).
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