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

2004/01/21 by Ming S. Liu, Liu, Ming S., B. D. Todd +3
Biochemistry, Genetics and Molecular Biology · #Biomolecules (q-bio.BM) #FOS: Biological sciences #Genomics (q-bio.GN) #q-bio.BM #q-bio.GN

paper · pdf · doi:10.48550/arxiv.q-bio/0401027

18pages, 4 figures

arxiv created 2004/01/21 · arxiv updated 2009/12/01

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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