• DOI:10.1038/emboj.2009.213
Corpus ID: 10606345

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

@article{Dueser200936SS,
  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},
  year={2009},
  volume={28}
}

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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