Spotlighting motors and controls of single FoF1-ATP synthase.

@article{Brsch2013SpotlightingMA,
  title={Spotlighting motors and controls of single FoF1-ATP synthase.},
  author={Michael B{\"o}rsch and Thomas M. Duncan},
  journal={Biochemical Society transactions},
  year={2013},
  volume={41 5},
  pages={
          1219-26
        }
}
Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F1 structure of the Escherichia coli enzyme with the ϵ-subunit in an inhibitory conformation initiated… 

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