Genetic evidence for the existence of two quinone related inhibitor binding sites in NADH-CoQ reductase.
Using the NADH-CoQ reductase of Rhodobacter capsulatus as a model for the mitochondrial Complex I, we have for the first time isolated bacterial mutants resistant to piericidin-A, a classical inhibitor of the mitochondrial enzyme. Their sensitivity to other inhibitors directed towards the quinone binding domain of complex I gives direct genetic evidence for the existence of two inhibitor binding sites.
Darrouzet
E
E
Département de Biologie Moléculaire et Structurale, CEA Grenoble, France.
Dupuis
A
A
D001665:Binding Sites; D042967:Electron Transport Complex I; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005663:Furans / Q000494:pharmacology; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011725:Pyridines / Q000494:pharmacology; D016354:Rhodobacter capsulatus; D012402:Rotenone / Q000494:pharmacology
D004791:Enzyme Inhibitors; D005663:Furans; D009097:Multienzyme Complexes; D011725:Pyridines; D012402:Rotenone; C061022:bullatacin; C100213:piericidin A; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D042967:Electron Transport Complex I