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

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dc.creatorLiu, Ming S.
dc.creatorTodd, B. D.
dc.creatorSadus, Richard J.
dc.date2004-01-21
dc.date.accessioned2026-07-07T05:58:08Z
dc.date.available2026-07-07T05:58:08Z
dc.descriptionF1-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.
dc.description18pages, 4 figures
dc.identifierhttps://arxiv.org/abs/q-bio/0401027
dc.identifierhttp://arxiv.org/abs/q-bio/0401027
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88247
dc.subjectGenomics
dc.subjectBiomolecules
dc.titleComplex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor
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