Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase.

@article{Zimmermann2005MovementsOT,
  title={Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase.},
  author={B. A. Zimmermann and Manuel D{\'i}ez and Nawid Zarrabi and Peter Gr{\"a}ber and Michael B{\"o}rsch},
  journal={The EMBO journal},
  year={2005},
  volume={24 12},
  pages={2053-63}
}
F0F1-ATP synthases catalyze proton transport-coupled ATP synthesis in bacteria, chloroplasts, and mitochondria. In these complexes, the epsilon-subunit is involved in the catalytic reaction and the activation of the enzyme. Fluorescence-labeled F0F1 from Escherichia coli was incorporated into liposomes. Single-molecule fluorescence resonance energy transfer (FRET) revealed that the epsilon-subunit rotates stepwise showing three distinct distances to the b-subunits in the peripheral stalk… CONTINUE READING

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