Regulatory role of the ATPase inhibitor protein on proton conduction by mitochondrial H+-ATPase complex.
This study shows that the natural inhibitor protein of mitochondrial H+-ATPase complex (IF1) inhibits, in addition to the catalytic activity, the proton conductivity of the complex. The inhibition of ATPase activity by IF1 is less effective in the purified F1 than in submitochondrial particles where F1 is bound to F0. No inhibition of H+ conductivity by F0 is observed in F1-depleted particles.
D000693:Anaerobiosis; D000818:Animals; D002417:Cattle; D006207:Half-Life; D008929:Mitochondria, Heart / Q000648:ultrastructure; D011188:Potassium / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000201:enzymology; D000097795:ATPase Inhibitory Protein
D011188:Potassium; D011506:Proteins; D006180:Proton-Translocating ATPases; D000097795:ATPase Inhibitory Protein