Studies on the molecular basis of H+ translocation by cytochrome c oxidase.
We report here studies which characterize further the interaction of N,N'-dicyclohexylcarbodiimide with cytochrome c oxidase leading to inhibition of H+ translocation by the enzyme. Further evidence is presented to show that the inhibition results from a real interaction of DCCD with the enzyme and cannot be accounted for by uncoupling and, contrary to recent criticisms, this interaction occurs specifically with subunit III of the enzyme even at relatively high inhibitor-to-enzyme stoichiometries. Use of a spin-label analogue of DCCD has enabled us to demonstrate that the carbodiimide-binding site is highly apolar and may not lie on the pathway of electron transfer.
D000818:Animals; D001693:Biological Transport, Active; D002417:Cattle; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D003576:Electron Transport Complex IV / Q000378:metabolism*; D000431:Ethanol / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D011485:Protein Binding
D000431:Ethanol; D004024:Dicyclohexylcarbodiimide; D003576:Electron Transport Complex IV