Pänke O, Rumberg B
Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität, Berlin, Germany.
FEBS Lett. 1996 Apr 1;383(3):196-200. doi: 10.1016/0014-5793(96)00246-3.
The rate of both ATP synthase and hydrolysis catalysed by the thiol-modulated and activated ATP synthase from spinach is measured as a function of all substrates including the protons inside the thylakoid lumen. The most important findings are: (1) sigmoid kinetics with respect to H+in, (2) hyperbolic kinetics with respect to ADP, ATP and phosphate, with Km for phosphate and ADP decreasing upon increasing H+in, (3) binding of ADP and phosphate in random order and competitive to ATP. Simulation of the complete set of experimental data is obtained by a kinetic model featuring Boyer's binding-chain mechanism.
对菠菜中硫醇调节并激活的ATP合酶所催化的ATP合成与水解速率进行了测定,该速率是所有底物(包括类囊体腔内部的质子)的函数。最重要的发现是:(1)相对于腔内质子(H⁺in)呈S形动力学;(2)相对于ADP、ATP和磷酸盐呈双曲线动力学,随着腔内质子(H⁺in)增加,磷酸盐和ADP的米氏常数(Km)降低;(3)ADP和磷酸盐以随机顺序结合且与ATP竞争。通过一个具有博耶结合链机制的动力学模型获得了对整套实验数据的模拟。