The reaction sites of rotenone and ubiquinone with mitochondrial NADH dehydrogenase.
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.
Singer
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Department of Biochemistry and Biophysics, University of California, San Francisco.
Ramsay
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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*
D011725:Pyridines; D012402:Rotenone; D014451:Ubiquinone; C100213:piericidin A; D009245:NADH Dehydrogenase