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Updated: Aug 24, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
Published on: January 22, 2019
Complex cooperativity of ATP hydrolysis in the F(1)-ATPase molecular motor
Ming S Liu1, B D Todd, Richard J Sadus
1Centre for Molecular Simulation, Swinburne University of Technology, PO Box 218, Hawthorn, Melbourne, Victoria 3122, Australia. ming@it.swin.edu.au
Abstract:
F(1)-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F(1)-ATPase does not follow the widely believed Michaelis-Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F(1)-ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F(1)-ATPase. This complexity may be taken into account to resolve the arguments on the binding change mechanism in F(1)-ATPase.
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