36° step size of proton‐driven c‐ring rotation in FoF1‐ATP synthase

  title={36° step size of proton‐driven c‐ring rotation in FoF1‐ATP synthase},
  author={M. Dueser and N. Zarrabi and D. Cipriano and S. Ernst and G. Glick and S. Dunn and M. B{\"o}rsch},
  journal={The EMBO Journal},
  • M. Dueser, N. Zarrabi, +4 authors M. Börsch
  • Published 2009
  • Biology, Medicine, Chemistry
  • The EMBO Journal
  • Synthesis of adenosine triphosphate ATP, the ‘biological energy currency’, 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. Although F1 uses 120° stepping during ATP synthesis, models of Fo predict either an incremental rotation of c subunits in 36° steps or larger step sizes comprising several fast substeps. Using single‐molecule fluorescence resonance energy… CONTINUE READING
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