The rotary mechanism sf ATP synthase

被引:258
作者
Stock, D
Gibbons, C
Arechaga, I
Leslie, AGW
Walker, JE
机构
[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England
[2] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
关键词
D O I
10.1016/S0959-440X(00)00147-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Since the chemiosmotic theory was proposed by Peter Mitchell in the 1960s, a major objective has been to elucidate the mechanism of coupling of the transmembrane proton motive force, created by respiration or photosynthesis, to the synthesis of ATP from ADP and inorganic phosphate. Recently, significant progress has been made towards establishing the complete structure of ATP synthase and revealing its mechanism. The X-ray structure of the F-1 catalytic domain has been completed and an electron density map of the F-1-c(10) subcomplex has provided a glimpse of the motor in the membrane domain. Direct microscopic observation of rotation has been extended to F-1-ATPase and F1Fo-ATPase complexes.
引用
收藏
页码:672 / 679
页数:8
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