dorsal/arxiv
View SchemaComplex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor
| Authors | Ming S. Liu, B. D. Todd, Richard J. Sadus |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0401027 |
| URL | https://arxiv.org/abs/q-bio/0401027 |
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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"abstract": "F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy\ninto mechanical rotation. The hydrolysis reaction in F1-ATPase does not follow\nthe widely believed Michaelis-Menten mechanism. Instead, the hydrolysis\nmechanism behaves in an ATP-dependent manner. We develop a model for enzyme\nkinetics and hydrolysis cooperativity of F1-ATPase which involves the\nbinding-state changes to the coupling catalytic reactions. The quantitative\nanalysis and modeling suggest the existence of complex cooperative hydrolysis\nbetween three different catalysis sites of F1-ATPase. This complexity may be\ntaken into account to resolve the arguments on the bindingchange mechanism in\nF1-ATPase.",
"arxiv_id": "q-bio/0401027",
"authors": [
"Ming S. Liu",
"B. D. Todd",
"Richard J. Sadus"
],
"categories": [
"q-bio.GN",
"q-bio.BM"
],
"title": "Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor",
"url": "https://arxiv.org/abs/q-bio/0401027"
},
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