Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochrome
Antimycin A
/ analogs & derivatives
Cytochrome b Group
/ genetics
Electron Spin Resonance Spectroscopy
Electron Transport Complex III
/ genetics
Hydrogen Bonding
Mitochondria
/ metabolism
Models, Molecular
Mutation
Oxidation-Reduction
Protein Conformation
Rhodobacter capsulatus
/ metabolism
Spectrum Analysis
/ methods
density functional theory
electron paramagnetic resonance
electron transfer
mitochondrial dysfunction
molecular dynamics simulations
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
17 08 2021
17 08 2021
Historique:
entrez:
14
8
2021
pubmed:
15
8
2021
medline:
15
12
2021
Statut:
ppublish
Résumé
Hemes are common elements of biological redox cofactor chains involved in rapid electron transfer. While the redox properties of hemes and the stability of the spin state are recognized as key determinants of their function, understanding the molecular basis of control of these properties is challenging. Here, benefiting from the effects of one mitochondrial disease-related point mutation in cytochrome
Identifiants
pubmed: 34389670
pii: 2026169118
doi: 10.1073/pnas.2026169118
pmc: PMC8379992
pii:
doi:
Substances chimiques
Cytochrome b Group
0
antimycin
11118-72-2
Antimycin A
642-15-9
Electron Transport Complex III
EC 7.1.1.8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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