Diverse reaction behaviors of artificial ubiquinones in mitochondrial respiratory complex I.
bioenergetics
chemical biology
complex I
mitochondria
ubiquinone
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
received:
02
02
2022
revised:
23
05
2022
accepted:
23
05
2022
pubmed:
2
6
2022
medline:
27
7
2022
entrez:
1
6
2022
Statut:
ppublish
Résumé
The ubiquinone (UQ) reduction step catalyzed by NADH-UQ oxidoreductase (mitochondrial respiratory complex I) is key to triggering proton translocation across the inner mitochondrial membrane. Structural studies have identified a long, narrow, UQ-accessing tunnel within the enzyme. We previously demonstrated that synthetic oversized UQs, which are unlikely to transit this narrow tunnel, are catalytically reduced by native complex I embedded in submitochondrial particles but not by the isolated enzyme. To explain this contradiction, we hypothesized that access of oversized UQs to the reaction site is obstructed in the isolated enzyme because their access route is altered following detergent solubilization from the inner mitochondrial membrane. In the present study, we investigated this using two pairs of photoreactive UQs (pUQ
Identifiants
pubmed: 35643318
pii: S0021-9258(22)00515-4
doi: 10.1016/j.jbc.2022.102075
pmc: PMC9243180
pii:
doi:
Substances chimiques
Ubiquinone
1339-63-5
Electron Transport Complex I
EC 7.1.1.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102075Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.