F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps

@article{Yasuda1998F1ATPaseIA,
  title={F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps},
  author={Ryohei Yasuda and Hiroyuki Noji and Kazuhiko Kinosita and Masasuke Yoshida},
  journal={Cell},
  year={1998},
  volume={93},
  pages={1117-1124}
}
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It appears that the presence of the slow β subunit(s) does not seriously affect other normal β subunits in the same F1-ATPase molecule and that the order of sequential catalytic events is faithfully maintained even when ATP binding to one or two of the catalytic sites is retarded.
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The novel function of the epsilon subunit as a coupling factor of ATP synthesis catalysed by F1 was revealed and the possible mechanism for highly coupled ATP synthesis supported by the ePSilon sub unit is discussed.
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Rotation of the γ Subunit in F1-ATPase; Evidence That ATP Synthase Is a Rotary Motor Enzyme
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