36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase

Details 36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase 36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase

2009-03-01

arxiv.org/abs/0903.0184v1

Biology

Quantitative Biology

Biomolecules

8 pages, 1 figure

Scientific paper

Synthesis of the biological "energy currency molecule" adenosine triphosphate ATP is accomplished by FoF1-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the Fo motor powers catalysis in the F1 motor. While F1 uses 120 degree stepping, Fo models predict a step-by-step rotation of c subunits 36 degree at a time, which is here demonstrated by single-molecule fluorescence resonance energy transfer.

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