Kinetic modelling of the proton translocating CF0CF1‐ATP synthase from spinach

FEBS Letters

Pänke, Oliver¹  Rumberg, Bernd¹ 

[1] Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität, D-10623 Berlin, Germany

关键词: Chloroplast;    ATP synthase;    Photophosphorylation;    Enzyme kinetics;   

DOI  :  10.1016/0014-5793(96)00246-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The rate of both ATP synthesis 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 K _m 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-change mechanism.

【 授权许可】

Unknown