Oster G, Wang H
Department of Molecular and Cellular Biology and College of Natural Resources, University of California, Berkeley, CA 94720-3112, USA.
Biochim Biophys Acta. 2000 May 31;1458(2-3):482-510. doi: 10.1016/s0005-2728(00)00096-7.
ATP synthase comprises two rotary motors in one. The F(1) motor can generate a mechanical torque using the hydrolysis energy of ATP. The F(o) motor generates a rotary torque in the opposite direction, but it employs a transmembrane proton motive force. Each motor can be reversed: The F(o) motor can drive the F(1) motor in reverse to synthesize ATP, and the F(1) motor can drive the F(o) motor in reverse to pump protons. Thus ATP synthase exhibits two of the major energy transduction pathways employed by the cell to convert chemical energy into mechanical force. Here we show how a physical analysis of the F(1) and F(o) motors can provide a unified view of the mechanochemical principles underlying these energy transducers.
ATP合酶由两个旋转马达构成一个整体。F(1)马达利用ATP水解能量产生机械扭矩。F(o)马达则利用跨膜质子动力产生相反方向的旋转扭矩。每个马达都可以反转：F(o)马达可以反向驱动F(1)马达合成ATP，F(1)马达也可以反向驱动F(o)马达泵送质子。因此，ATP合酶展现了细胞用于将化学能转化为机械力的两种主要能量转换途径。在此，我们展示了对F(1)和F(o)马达的物理分析如何能为这些能量转换器背后的机械化学原理提供统一的视角。
