Molecular Dynamics Analysis of Inhibitor Binding Interactions in the Vibrio cholerae Respiratory Complex NQR.

ABSTRACT: The sodium-pumping ubiquinone oxidoreductase sodium pumping quinone reductase (NQR) is an important enzyme in the respiratory chain of multiple pathogenic gram-negative bacteria. NQR has been proposed as a viable antibiotic target due to its importance in supporting energy-consuming reactions and its absence in human cells. In this study, molecular dynamics simulations were conducted to characterize the interactions between the ubiquinone binding pocket of Vibrio cholerae NQR with its substrate analogue ubiquinone-4 and three potent inhibitors: HQNO, aurachin-D42, and korormicin-A. Through interaction fingerprinting, distance calculations, and clustering analysis, important binding motifs for each of these ligands were identified. Subunit B residues K54, F137, E144, V145, V155, E157, G158,

SUBMITTER: DePaolo-Boisvert JA 

PROVIDER: S-EPMC12779168 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature