Docking and molecular simulations reveal a quinone-binding site on the surface of respiratory complex I.
FEBS Lett
; 596(9): 1133-1146, 2022 05.
Article
em En
| MEDLINE
| ID: mdl-35363885
ABSTRACT
The first component of the mitochondrial electron transport chain is respiratory complex I. Several high-resolution structures of complex I from different species have been resolved. However, despite these significant achievements, the mechanism of redox-coupled proton pumping remains elusive. Here, we combined atomistic docking, molecular dynamics simulations, and site-directed mutagenesis on respiratory complex I from Yarrowia lipolytica to identify a quinone (Q)-binding site on its surface near the horizontal amphipathic helices of ND1 and NDUFS7 subunits. The surface-bound Q makes stable interactions with conserved charged and polar residues, including the highly conserved Arg72 from the NDUFS7 subunit. The binding and dynamics of a Q molecule at the surface-binding site raise interesting possibilities about the mechanism of complex I, which are discussed.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Yarrowia
/
Complexo I de Transporte de Elétrons
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
Finlândia