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F1-ATPase-Catalyzed Synthesis of ATP from Oleoylphosphate and ADP
Richard Johnston and Richard S. Criddle
Proceedings of the National Academy of Sciences of the United States of America
Vol. 74, No. 11 (Nov., 1977), pp. 4919-4923
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/67495
Page Count: 5
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Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 126.96.36.199) isolated from yeast mitochondria catalyze the reaction of oleoylphosphate with ADP to yield ATP and oleic acid. Formation of ATP is specifically inhibited by the F1-ATPase inhibitor 1799 and by dinitrophenol. In the presence of F1, dinitrophenol ``uncouples'' the synthase reaction by causing rapid hydrolysis of oleoylphosphate without ATP formation. It is proposed that this F1-catalyzed ATP synthesis reaction corresponds to the terminal chemical step in oxidative phosphorylation.
Proceedings of the National Academy of Sciences of the United States of America © 1977 National Academy of Sciences