Abstract
This study shows that the natural inhibitor protein of mitochondrial H +-ATPase complex (IF 1) inhibits, in addition to the catalytic activity, the proton conductivity of the complex. The inhibition of ATPase activity by IF 1 is less effective in the purified F 1 than in submitochondrial particles where F 1 is bound to F 0. No inhibition of H + conductivity by F 0 is observed in F 1-depleted particles
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