Yinghao Zhang, Jun Wang, Yuanbo Cui, Jiachang Yue, Xiaohong Fang
The National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Biochem Biophys Res Commun. 2005 May 27;331(1):370-4. doi: 10.1016/j.bbrc.2005.03.172.
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.
我们尝试直接观察F₀F₁ - ATP合酶的光驱动旋转。F₀F₁ - ATP合酶的F₀缺失δ亚基与细菌视紫红质（BRs）共同重组到脂质体中。BR将辐射能转化为质子的电化学梯度以驱动F₀F₁ - ATP合酶。因此，通过荧光显微镜，利用连接到β亚基的荧光肌动蛋白丝作为其取向标记，直接观察到了F₀F₁ - ATP合酶的光驱动旋转。F₀合酶的旋转扭矩值计算为27.93±1.88皮牛纳米。在纳米器件的开发中，ATP合酶有望成为一种有前景的旋转分子马达。
