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New concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
The P/sub i/ reversible HOH exchange reaction of oxidative phosphorylation is considerably less sensitive to uncouplers than the P/sub i/ reversible ATP and ATP reversible HOH exchanges. The uncoupler-insensitive P/sub i/ reversible HOH exchange is inhibited by oligomycin. These results and other considerations suggest that the relatively rapid and uncoupler-insensitive P/sub i/ reversible HOH exchange results from a rapid, reversible hydrolysis of a tightly but noncovalently bound ATP at a catalytic site for oxidative phosphorylation, concomitant with interchange of medium and bound P/sub i/. Such tightly bound ATP has been demonstrated in submitochondrial particles in the presence of uncouplers, P/sub i/, and ADP, by rapid labeling from /sup 32/P/sub i/ under essentially steady-state phosphorylation conditions. These results lead to the working hypothesis that in oxidative phosphorylation energy from electron transport causes release of preformed ATP from the catalytic site. This release could logically involve energy-requiring protein conformational change.
OSTI ID:
7279480
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 70:10; ISSN PNASA
Country of Publication:
United States
Language:
English