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Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F0F1): Direct Observation

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Science  26 Nov 1999:
Vol. 286, Issue 5445, pp. 1722-1724
DOI: 10.1126/science.286.5445.1722

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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.

  • * Present address: Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22906–0011, USA.

  • To whom correspondence should be addressed. E-mail: m-futai{at}sanken.osaka-u.ac.jp

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