Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10771442 | Biochemical and Biophysical Research Communications | 2005 | 5 Pages |
Abstract
We have attempted direct observation of the light-driven rotation of a FoF1-ATP motor. The FoF1-ATP motor was co-reconstituted by the deletion-δ subunit of FoF1-ATP synthase with bacteriorhodopsins (BRs) into a liposome. The BR converts radiation energy into electrochemical gradient of proton to drive the FoF1-ATP motor. Therefore, the light-driven rotation of FoF1-ATP motor has been directly observed by a fluorescence microscopy using a fluorescent actin filament connected to β-subunit as a marker of its orientation. The rotational torque value of the Fo motor was calculated as 27.93 ± 1.88 pN nm. The ATP motor is expected to be a promising rotary molecular motor in the development of nanodevices.
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Authors
Zhang Yinghao, Wang Jun, Cui Yuanbo, Yue Jiachang, Fang Xiaohong,