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

被引：29

作者：

Panke, O ^{[1
]}

Rumberg, B ^{[1
]}

机构：

[1] TECH UNIV BERLIN,MAX VOLMER INST BIOPHYS & PHYS CHEM,D-10623 BERLIN,GERMANY

来源：

FEBS LETTERS | 1996年 / 383卷 / 03期

关键词：

chloroplast; ATP synthase; photophosphorylation; enzyme kinetics;

D O I：

10.1016/0014-5793(96)00246-3

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：

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.

引用

页码：196 / 200

页数：5

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