[Interaction of ATPase from submitochondrial fragments and a natural inhibitor protein during delta-mu-H+ generation on a membrane].
An addition of the inhibitor protein (IF1) to submitochondrial particles (SMP) essentially free of endogenous IF1 (AS-SMP) results in a synchroneous inhibition of ATP hydrolysis and ATP-dependent reduction of NAD+ by succinate without any effect on the oxidative phosphorylation rate. The binding of IF1 to the membrane-bound ATPase leads to the loss of the inhibitor protein sensitivity to trypsin despite the delta mu H+ generation. The data obtained are consistent with a model according to which there exist the hydrolase and synthetase forms of F1 and contradict the generally accepted concepts on the delta mu H+-dependent dissociation of the F1-IF1 complex.
Vasil'eva
E A
EA
Panchenko
M V
MV
Vinogradov
A D
AD
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors; D002417:Cattle; D004579:Electron Transport; D006868:Hydrolysis; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology; D010084:Oxidation-Reduction; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000201:enzymology*; D000097795:ATPase Inhibitory Protein
D000251:Adenosine Triphosphatases; D000252:Calcium-Transporting ATPases; D011506:Proteins; D000097795:ATPase Inhibitory Protein
Vzaimodeĭstvie ATPazy submitokhondrial'nykh fragmentov i prirodnogo belka-ingibitora v usloviiakh generatsii delta-mu-H+ na membrane.