The effect of Mg2+ on mitochondrial F0.F1 ATPase and characteristics of the nucleotide binding sites.
The interaction of Mg2+ with nucleotide-washed F0.F1 ATPase from pig heart was studied. Mg2+ had no effect on nucleotide-washed F0.F1 ATPase, but it competitively inhibited the hydrolytic activity of washed F0.F1 ATPase preincubated with ADP and slightly activated the hydrolytic activity of washed F0.F1 ATPase preincubated with ATP. In the last two cases, it revealed negative cooperativity. The effect of Mg2+ on F0.F1 ATPase is therefore closely related to the characteristics of the nucleotide binding sites on mitochondrial F0.F1 ATPase.
Ye
J J
JJ
Institute of Biophysics, Academia Sinica, Beijing, China.
Du
J
J
Lin
Z H
ZH
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D004789:Enzyme Activation; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013552:Swine
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D008274:Magnesium