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Keeping up with the F1-ATPase

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  • Howard C. Berg

    (Harvard University
    Rowland Institute for Science)

Abstract

Just over a year ago, Kazuhiko Kinosita and colleagues reported that they could visualize rotation of the F1-ATPase by tethering an actin filament to the γ-subunit and watching it spin. Now they've taken that work a step further, and in their latest study report that the F1-ATPase rotates its actin tag in discrete 120° steps. Not only that, but the work done by each step is close to the energy available from hydrolysing one molecule of ATP —translating to almost 100% efficiency.

Suggested Citation

  • Howard C. Berg, 1998. "Keeping up with the F1-ATPase," Nature, Nature, vol. 394(6691), pages 324-325, July.
    • Handle: RePEc:nat:nature:v:394:y:1998:i:6691:d:10.1038_28506
    DOI: 10.1038/28506
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