Structural insights into functional properties of the oxidized form of cytochrome c oxidase.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
16 09 2023
16 09 2023
Historique:
received:
05
04
2023
accepted:
07
09
2023
medline:
18
9
2023
pubmed:
17
9
2023
entrez:
16
9
2023
Statut:
epublish
Résumé
Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable O
Identifiants
pubmed: 37717031
doi: 10.1038/s41467-023-41533-x
pii: 10.1038/s41467-023-41533-x
pmc: PMC10505203
doi:
Substances chimiques
Electron Transport Complex IV
EC 1.9.3.1
Protons
0
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5752Informations de copyright
© 2023. Springer Nature Limited.
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