一种可溶的线粒体ATP合成酶复合体，催化ATP-磷酸和ATP-ADP交换。
A soluble mitochondrial ATP synthetase complex catalyzing ATP-phosphate and ATP-ADP exchange.
作者信息
Fisher R J, Chen J C, Sani B P, Kaplay S S, Sanadi D R
出版信息
Proc Natl Acad Sci U S A. 1971 Sep;68(9):2181-4. doi: 10.1073/pnas.68.9.2181.
The highly purified soluble ATP synthetase complex from mitochondria, containing energy-transfer Factor A (the terminal ADP phosphorylation enzyme of oxidative phosphorylation) and Factor D, catalyzes ATP-P(i) and ATP-ADP exchange reactions. The ATP-P(i) exchange activity is inhibited by low concentrations of the uncouplers of oxidative phosphorylation, oligomycin and p-chloromercnriphenylsulfonate. It is stimulated threefold by dithiothreitol and is Mg(++) dependent. Antiserum to coupling factor 1 (F(1)) also inhibits the ATP-P(i) exchange. The ATP-ADP exchange activity appears to be greater than the ATP-P(i) exchange activity. The results suggest that the nonphosphorylated high-energy intermediate (X approximately C), and possibly the phosphorylated intermediate (X approximately P), are formed on the synthetase. Sites of uncoupler and oligomycin action reside in the terminal ATP synthetase.
来自线粒体的高度纯化的可溶性ATP合酶复合物，含有能量转移因子A（氧化磷酸化的末端ADP磷酸化酶）和因子D，催化ATP-P(i)和ATP-ADP交换反应。ATP-P(i)交换活性受到低浓度氧化磷酸化解偶联剂、寡霉素和对氯汞基苯磺酸盐的抑制。它受到二硫苏糖醇的三倍刺激，并且依赖于Mg(++)。针对偶联因子1（F(1)）的抗血清也抑制ATP-P(i)交换。ATP-ADP交换活性似乎大于ATP-P(i)交换活性。结果表明，在合成酶上形成了非磷酸化的高能中间体（X≈C），可能还有磷酸化中间体（X≈P）。解偶联剂和寡霉素的作用位点位于末端ATP合酶中。
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