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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
Stable URL: http://www.jstor.org/stable/67495
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
F1-ATPase-Catalyzed Synthesis of ATP from Oleoylphosphate and ADP
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Abstract

Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 3.6.1.3) 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.

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