Differential inhibition of F0F1-ATPase-catalysed reactions in bovine-heart submitochondrial particles by organotin compounds.
Preincubation of coupled submitochondrial particles with low concentrations of triorganotin compounds results in complete inhibition of the oligomycin-sensitive ATPase activity without any significant effect on the rate of succinate-driven ATP synthesis. The residual ATP synthetic activity is inhibited by oligomycin and uncouplers. The differential inhibition of ATP synthesis and hydrolysis by the triorganotin compounds examined suggests that the two processes are not 'mirror images' of each other, but that they occur through different routes and that the F1F0-ATPase is at least bifunctional.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D002417:Cattle; D004579:Electron Transport; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D006180:Proton-Translocating ATPases; D013367:Submitochondrial Particles / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D014220:Trialkyltin Compounds / Q000494:pharmacology*
D013438:Sulfhydryl Compounds; D014220:Trialkyltin Compounds; C015129:dibutylchloro(chloromethyl)tin; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases