保罗.博耶(P.D.Boyer)教授为阐明ATP酶作用机制所提出的结合变化机制有两个基本要点:一是ATP合成所需要的能量原则上是用于促进酶上紧密结合的ATP的释放和无机磷、ADP的结合;二是在净ATP形成过程中,酶上的各催化部位是高度协同地顺序起作用的.γ亚基在F1-ATP酶中的旋转运动使三个催化部位构象不对称是实现结合变化的基础.高分辨率牛心线粒体F1-ATP酶的晶体结构发表以后,出现了一些支持旋转催化机制的直接实验证据.
The binding change mechanism for the ATP synthase has two central features. One is that the principle use of energy required for ATP synthesis is to promote the release of tightly bound ATP and the binding of Pi and ADP in a manner competent to form bound ATP. The second is that during net ATP formation multiple catalytic sites on the synthase participate in strongly cooperative sequence. Rotation of the γ subunit in F1 is thought to deform the catalytic sites to give binding change. When the crystal structure of the F1-ATPase was eventually solved, direct evidences for rotation of subunits during catalysis of F1-ATPase were provided.
周筠梅. ATP合成酶的结合变化机制和旋转催化——1997年诺贝尔化学奖的部分工作介绍[J].生物化学与生物物理进展,1998,25(1):9-17
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