Quinone chemistry in respiratory complex I involves protonation of a conserved aspartic acid residue.
Escherichia coli
NADH dehydrogenase
NADH:quinone oxidoreductase
iron–sulfur cluster
proton‐coupled electron transfer
quinone reduction
redox‐induced FTIR spectroscopy
site‐directed mutagenesis
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
11 Sep 2024
11 Sep 2024
Historique:
revised:
22
08
2024
received:
05
08
2024
accepted:
23
08
2024
medline:
12
9
2024
pubmed:
12
9
2024
entrez:
12
9
2024
Statut:
aheadofprint
Résumé
Respiratory complex I is a central metabolic enzyme coupling NADH oxidation and quinone reduction with proton translocation. Despite the knowledge of the structure of the complex, the coupling of both processes is not entirely understood. Here, we use a combination of site-directed mutagenesis, biochemical assays, and redox-induced FTIR spectroscopy to demonstrate that the quinone chemistry includes the protonation and deprotonation of a specific, conserved aspartic acid residue in the quinone binding site (D325 on subunit NuoCD in Escherichia coli). Our experimental data support a proposal derived from theoretical considerations that deprotonation of this residue is involved in triggering proton translocation in respiratory complex I.
Identifiants
pubmed: 39262040
doi: 10.1002/1873-3468.15013
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : 278002225/RTG 2202
Organisme : Deutsche Forschungsgemeinschaft
ID : FR1140/11-2
Organisme : Agence Nationale de la Recherche
ID : ANR-10-LABX-0026_CSC
Informations de copyright
© 2024 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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