期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：9
页码：2181-2184
DOI：10.1073/pnas.68.9.2181
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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-Pi and ATP-ADP exchange reactions. The ATP-Pi 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 (F1) also inhibits the ATP-Pi exchange. The ATP-ADP exchange activity appears to be greater than the ATP-Pi exchange activity. The results suggest that the nonphosphorylated high-energy intermediate (X[~]C), and possibly the phosphorylated intermediate (X[~]P), are formed on the synthetase. Sites of uncoupler and oligomycin action reside in the terminal ATP synthetase.
关键词：oligomycin ; p -chloromercuriphenylsulfonate ; high-energy intermediate ; uncoupling
