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Updated: Aug 9, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Kinetic modelling of the proton translocating CF0CF1-ATP synthase from spinach
1Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität, Berlin, Germany.
Abstract:
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.
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