Keeping up with the F1-ATPase

Howard C. Berg ()
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Howard C. Berg: Harvard University

Nature, 1998, vol. 394, issue 6691, 324-325

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.

Date: 1998
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DOI: 10.1038/28506

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