NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH: Quinone oxidoreductase from vibrio cholerae

Journal of Biological Chemistry

Volumn 288, Issue 42, 2013, Pages 30597-30606

  Nedielkov, Ruslan ^a   Steffen, Wojtek ^b   Steuber, Julia ^b   Möller, Heiko Maa ^a  

^a UNIVERSITY OF KONSTANZ   (Germany)

^b UNIVERSITY OF HOHENHEIM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; CATALYTIC MECHANISMS; ELECTRON-TRANSFER STEP; EXPERIMENTAL EVIDENCE; OXIDOREDUCTASES; SIMULTANEOUS BINDINGS; VIBRIO CHOLERAE;

SODIUM;

LIGANDS;

2 HEPTYL 4 HYDROXYQUINOLINE 1 OXIDE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (QUINONE); SODIUM ION; TRYPTOPHAN;

ARTICLE; BINDING SITE; CATALYSIS; CHLOROPLAST; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRON TRANSPORT; LIGAND BINDING; MITOCHONDRION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; VIBRIO CHOLERAE;

DBMIB; INTERLIGAND NOE; MEMBRANE ENZYMES; NMR; REDOX; SODIUM TRANSPORT; UBIQUINONE;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; DIBROMOTHYMOQUINONE; HYDROXYQUINOLINES; MAGNETIC RESONANCE SPECTROSCOPY; NAD; PROTEIN SUBUNITS; QUINONE REDUCTASES; UBIQUINONE; VIBRIO CHOLERAE;

EID: 84886931827     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.435750     Document Type: Article

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