文章基本信息

标题：A New Concept for Energy Coupling in Oxidative Phosphorylation Based on a Molecular Explanation of the Oxygen Exchange Reactions
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作者：Paul D. Boyer ; Richard L. Cross ; William Momsen 等
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：1973
卷号：70
期号：10
页码：2837-2839
DOI：10.1073/pnas.70.10.2837
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The Pi {rightleftarrows} HOH exchange reaction of oxidative phosphorylation is considerably less sensitive to uncouplers than the Pi {rightleftarrows} ATP and ATP {rightleftarrows} HOH exchanges. The uncoupler-insensitive Pi {rightleftarrows} HOH exchange is inhibited by oligomycin. These results and other considerations suggest that the relatively rapid and uncoupler-insensitive Pi {rightleftarrows} 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 Pi. Such tightly bound ATP has been demonstrated in submitochondrial particles in the presence of uncouplers, Pi, and ADP, by rapid labeling from 32Pi 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.
关键词：protein conformational change ; uncouplers ; mitochondria