title: The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase.
abstract: This article summarizes recent studies in the authors' and other laboratories of selective inhibitors acting at the 'rotenone' site and at the Q binding site in the NADH-Q oxidoreductase segment of the respiratory chain. A wide array of inhibitors act at the rotenone site to block electron flux from the enzyme to the Q pool. Using evidence from studies with rotenone, piericidin A, and analogs of the neurotoxic N-methyl-4-phenylpyridinium, we have proposed two binding sites for these inhibitors, both of which must be occupied for complete inhibition of NADH oxidation.
authors.affiliation: Department of Biochemistry and Biophysics, University of California, San Francisco.
authors.forename: T P
authors.initials: TP
authors.lastname: Singer
authors.forename: R R
authors.initials: RR
authors.lastname: Ramsay
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D008928:Mitochondria / Q000187:drug effects / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology; D009245:NADH Dehydrogenase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D011725:Pyridines / Q000494:pharmacology; D012402:Rotenone / Q000494:pharmacology*; D014451:Ubiquinone / Q000494:pharmacology*
chemical_list: D011725:Pyridines; D012402:Rotenone; D014451:Ubiquinone; C100213:piericidin A; D009245:NADH Dehydrogenase