Identification of the Catalytic Ubiquinone-binding Site of Vibrio cholerae Sodium-dependent NADH Dehydrogenase: A NOVEL UBIQUINONE-BINDING MOTIF.

ABSTRACT: The sodium-dependent NADH dehydrogenase (Na⁺-NQR) is a key component of the respiratory chain of diverse prokaryotic species, including pathogenic bacteria. Na⁺-NQR uses the energy released by electron transfer between NADH and ubiquinone (UQ) to pump sodium, producing a gradient that sustains many essential homeostatic processes as well as virulence factor secretion and the elimination of drugs. The location of the UQ binding site has been controversial, with two main hypotheses that suggest that this site could be located in the cytosolic subunit A or in the membrane-bound subunit B. In this work, we performed alanine scanning mutagenesis of aromatic residues located in transmembrane helices II, IV, and V of subunit B, near glycine residues 140 and 141. These two cr

SUBMITTER: Tuz K 

PROVIDER: S-EPMC5314197 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature