Capaldi Roderick A, Aggeler Robert
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA.
Trends Biochem Sci. 2002 Mar;27(3):154-60. doi: 10.1016/s0968-0004(01)02051-5.
The F(1)F(0)-type ATP synthase is a key enzyme in cellular energy interconversion. During ATP synthesis, this large protein complex uses a proton gradient and the associated membrane potential to synthesize ATP. It can also reverse and hydrolyze ATP to generate a proton gradient. The structure of this enzyme in different functional forms is now being rapidly elucidated. The emerging consensus is that the enzyme is constructed as two rotary motors, one in the F(1) part that links catalytic site events with movements of an internal rotor, and the other in the F(0) part, linking proton translocation to movements of this F(0) rotor. Although both motors can work separately, they must be connected together to interconvert energy. Evidence for the function of the rotary motor, from structural, genetic and biophysical studies, is reviewed here, and some uncertainties and remaining mysteries of the enzyme mechanism are also discussed.
F(1)F(0)型ATP合酶是细胞能量转换中的关键酶。在ATP合成过程中，这种大型蛋白质复合物利用质子梯度和相关的膜电位来合成ATP。它也可以逆转并水解ATP以产生质子梯度。目前，这种酶在不同功能形式下的结构正在迅速得到阐明。新形成的共识是，该酶由两个旋转马达构成，一个在F(1)部分，将催化位点事件与内部转子的运动联系起来，另一个在F(0)部分，将质子转运与该F(0)转子的运动联系起来。尽管两个马达可以单独工作，但它们必须连接在一起才能实现能量的相互转换。本文综述了来自结构、遗传和生物物理研究的关于旋转马达功能的证据，同时也讨论了该酶机制中一些不确定因素和仍存在的谜团。
