The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.

@article{Omote1999TheGR,
  title={The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.},
  author={Hiroshi Omote and N Sambonmatsu and Kyoko Saito and Yoshihiro Sambongi and Atsuko Iwamoto-Kihara and Toshio Yanagida and Yoh Wada and Masamitsu Futai},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 14},
  pages={7780-4}
}
The rotation of the gamma-subunit has been included in the binding-change mechanism of ATP synthesis/hydrolysis by the proton ATP synthase (FOF1). The Escherichia coli ATP synthase was engineered for rotation studies such that its ATP hydrolysis and synthesis activity is similar to that of wild type. A fluorescently labeled actin filament connected to the gamma-subunit of the F1 sector rotated on addition of ATP. This progress enabled us to analyze the gammaM23K (the gamma-subunit Met-23… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 28 extracted citations

High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences • 2013

Similar Papers

Loading similar papers…