title: Kinetics of interaction between the H+-translocating component of the mitochondrial ATPase complex and oligomycin or dicyclohexylcarbodiimide.
abstract: Kinetics of interaction between the H+-translocating component of the mitochondrial ATPase complex and oligomycin or dicyclohexylcarbodiimide were studied in beef heart submitochondrial particles, and the results suggest that the two inhibitors have different binding sites with respect to the membrane and to F1. Oligomycin seems to be bound to a subunit or a part of a subunit in F0, which is localized superficially, and which is influenced by F1, since the presence of F1 considerably lowers the rate of inhibition. The oligomycin binding site further seems to be influenced by the different conformational states of F1 occurring during the catalytic cycle of the enzyme. The binding site of DCCD on F0, on the other hand, seems to be deeply embedded in the membrane and not influenced by F1.
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D002234:Carbodiimides / Q000494:pharmacology*; D002417:Cattle; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000187:drug effects / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D009840:Oligomycins / Q000494:pharmacology*; D006180:Proton-Translocating ATPases; D013367:Submitochondrial Particles / Q000187:drug effects / Q000201:enzymology
chemical_list: D002234:Carbodiimides; D009097:Multienzyme Complexes; D009840:Oligomycins; D004024:Dicyclohexylcarbodiimide; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases