Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0 F 1 ): Direct Observation
- 26 November 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 286 (5445) , 1722-1724
- https://doi.org/10.1126/science.286.5445.1722
Abstract
F0F1, found in mitochondria or bacterial membranes, synthesizes adenosine 5′-triphosphate (ATP) coupling with an electrochemical proton gradient and also reversibly hydrolyzes ATP to form the gradient. An actin filament connected to a c subunit oligomer of F0 was able to rotate by using the energy of ATP hydrolysis. The rotary torque produced by the c subunit oligomer reached about 40 piconewton-nanometers, which is similar to that generated by the γ subunit in the F1 motor. These results suggest that the γ and c subunits rotate together during ATP hydrolysis and synthesis. Thus, coupled rotation may be essential for energy coupling between proton transport through F0 and ATP hydrolysis or synthesis in F1.Keywords
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