Kinetic modelling of the proton translocating CF0CF1‐ATP synthase from spinach
- 1 April 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 383 (3), 196-200
- https://doi.org/10.1016/0014-5793(96)00246-3
Abstract
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 Hin +, (2) hyperbolic kinetics with respect to ADP, ATP and phosphate, with K m for phosphate and ADP decreasing upon increasing Hin +, (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.Keywords
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