Specificity of acidic phospholipids (CL & PA) in the activation of mitochondrial F0F1 ATPase by Mg2+.
The interaction of Mg2+ with native F0F1 ATPase was studied. The hydrolytic activity of F0F1 ATPase could be competitively activated by Mg2+, but the preincubation of F0F1 ATPase with cholate eliminated the Mg2+ effect. The result from the comparison of the effect of Mg2+ on F0F1 ATPase with that on soluble F1 ATPase, and the fact that the activation of Mg2+ on cholate-treated F0F1 ATPase could be reconstituted only by divalent acidic phospholipid cardiolipin, indicate that there exists a specificity between the acidic phospholipids of the mitochondrial inner membrane and Mg2+ enhancement of ATP-hydrolyzing activity of F0F1 ATPase.
Ye
J J
JJ
Institute of Biophysics, Academia Sinica, Beijing, P.R.C.
Lin
Z H
ZH
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002308:Cardiolipins / Q000494:pharmacology*; D019826:Cholic Acid; D002793:Cholic Acids / Q000494:pharmacology; D002855:Chromatography, Thin Layer; D004789:Enzyme Activation / Q000187:drug effects; D006868:Hydrolysis; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D010712:Phosphatidic Acids / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013552:Swine
D002308:Cardiolipins; D002793:Cholic Acids; D010712:Phosphatidic Acids; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D019826:Cholic Acid; D008274:Magnesium