Molecular motors -: Keeping up with the F1-ATPase

被引：13

作者：

Berg, HC ^{[1
]}

机构：

[1] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA

[2] Harvard Univ, Dept Phys, Cambridge, MA 02138 USA

来源：

NATURE | 1998年 / 394卷 / 6691期

关键词：

D O I：

10.1038/28506

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学];

摘要：

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.

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页码：324 / 325

页数：2

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