Mechanism of the F1F0-type ATP synthase, a biological rotary motor

被引:289
作者
Capaldi, RA [1 ]
Aggeler, R [1 ]
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
关键词
D O I
10.1016/S0968-0004(01)02051-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The F1F0-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.
引用
收藏
页码:154 / 160
页数:7
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