Operation mechanism of F_oF_1-adenosine triphosphate synthase revealed by its structure and dynamics
Operation mechanism of F_oF_1-adenosine triphosphate synthase revealed by its structure and dynamics
复制标题
F_oF_1-三磷酸腺苷合酶的结构和动力学揭示其运行机制
作者：
Iino R;Noji H
FoF 1-三磷酸腺苷（ATP）合酶是两种旋转马达蛋白的复合物，将质子穿过细胞膜的电化学电势可逆地转化为ATP的磷酸转移电势，以提供细胞的能量流通。水溶性马达是F1-ATP酶，其具有ATP合成/水解催化位点。分离的F1水解ATP，使旋转轴相对于定子环旋转。膜嵌入式马达是Fo，其由质子流沿质子电化学电势向下驱动。在FoF 1复合物中，机械旋转、化学反应和质子运输的方向由ATP水解反应的吉布斯自由能和质子跨膜的电化学电势之间的相对振幅决定。因此，FoF 1-ATP合酶是一种高效的分子装置，其中化学，机械和势能紧密且可逆地转化。在这篇评论中，我们总结了我们的最新知识，这种复杂的纳米机器的运作机制，揭示了它的结构和动力学。© 2013 IUBMB Life，65（3）：238-246，2013。
FoF1‐Adenosine triphosphate (ATP) synthase, a complex of two rotary motor proteins, reversibly converts the electrochemical potential of protons across the cell membrane into phosphate transfer potential of ATP to provide the energy currency of the cell. The water‐soluble motor is F1‐ATPase, which possesses ATP synthesis/hydrolysis catalytic sites. Isolated F1hydrolyses ATP to rotate the rotary shaft against the stator ring. The membrane‐embedded motor is Fo, which is driven by proton flow down the proton electrochemical potential. In the FoF1complex, the direction of mechanical rotation, the chemical reaction, and the proton transport are determined by the relative amplitudes between the Gibbs free energy of the ATP hydrolysis reaction and the electrochemical potential of protons across the membrane. Therefore, FoF1‐ATP synthase is a highly efficient molecular device in which the chemical, mechanical, and potential energies are tightly and reversibly converted. In this critical review, we summarize our latest knowledge about the operation mechanism of this sophisticated nanomachine, revealed by its structure and dynamics. © 2013 IUBMB Life, 65(3):238–246, 2013.