# Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor

Source: [Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor](<https://www.sota2.com/research/paper/68fa5e881e209131ce9e3205>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-25T18:50:47.722Z

Authors: Ming S. Liu, B. D. Todd, Richard J. Sadus

Published: 2004-01-21T01:12:22.000Z

## Abstract

F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F1-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 F1-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 F1-ATPase. This complexity may be taken into account to resolve the arguments on the bindingchange mechanism in F1-ATPase.

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/q-bio/0401027>)

[PDF](<https://arxiv.org/pdf/q-bio/0401027.pdf>)