title: Rotary torque produced by proton motive force in FoF1 motor.
abstract: We have attempted direct observation of the light-driven rotation of a FoF(1)-ATP motor. The FoF(1)-ATP motor was co-reconstituted by the deletion-delta subunit of FoF(1)-ATP synthase with bacteriorhodopsins (BRs) into a liposome. The BR converts radiation energy into electrochemical gradient of proton to drive the FoF(1)-ATP motor. Therefore, the light-driven rotation of FoF(1)-ATP motor has been directly observed by a fluorescence microscopy using a fluorescent actin filament connected to beta-subunit as a marker of its orientation. The rotational torque value of the Fo motor was calculated as 27.93+/-1.88pNnm. The ATP motor is expected to be a promising rotary molecular motor in the development of nanodevices.
authors.affiliation: The National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Zhang
authors.initials: Z
authors.lastname: Yinghao
authors.forename: Wang
authors.initials: W
authors.lastname: Jun
authors.forename: Cui
authors.initials: C
authors.lastname: Yuanbo
authors.forename: Yue
authors.initials: Y
authors.lastname: Jiachang
authors.forename: Fang
authors.initials: F
authors.lastname: Xiaohong
mesh_terms: D008841:Actin Cytoskeleton / Q000502:physiology; D001436:Bacteriorhodopsins / Q000378:metabolism; D008027:Light; D008081:Liposomes; D008856:Microscopy, Fluorescence; D020409:Molecular Motor Proteins / Q000378:metabolism*; D018892:Proton-Motive Force; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D019415:Torque
chemical_list: D008081:Liposomes; D020409:Molecular Motor Proteins; D001436:Bacteriorhodopsins; D006180:Proton-Translocating ATPases