DIFFERENTIAL INHIBITION OF F0F1-ATPASE-CATALYZED 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 2 processes are not ''mirror images'' of each other, but that they occur through different routes and that the F1F0-ATPase is at least bifunctional.