Kinetics of ATP and inorganic phosphate release during hydrolysis of ATP by rabbit skeletal actomyosin subfragment 1:Oxygen exchange between water and ATP or phosphate

Bowater, Richard ORCID: https://orcid.org/0000-0002-2745-7807, Zimmerman, Robert W. and Webb, Martin R. (1990) Kinetics of ATP and inorganic phosphate release during hydrolysis of ATP by rabbit skeletal actomyosin subfragment 1:Oxygen exchange between water and ATP or phosphate. Journal of Biological Chemistry, 265 (1). pp. 171-176. ISSN 0021-9258

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Abstract

We have used the technique of phosphate:water oxygen exchange to measure the rate of ATP and Pi release and Pi binding to myosin subfragment 1 and actomyosin subfragment 1 from rabbit skeletal muscle. The oxygen exchange distributions for ATP and Pi release fit a simple kinetic model with a single set of rate constants for each step. For actomyosin subfragment 1 (20°C, pH 7.0, I = 50 mM), the rate constant governing ATP release is ∼8 s-1, Pi release is at ∼60 s-1 and Pi rebinds to an ADP state at >120 M-1 s-1. These rate constants are similar to those that may occur for undistorted cross-bridges within glycerinated rabbit psoas fibers (Bowater, R., Webb, M. R., and Ferenczi, M. A. (1989) J. Biol. Chem. 264, 7193-7201.

Item Type:	Article
Uncontrolled Keywords:	biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Related URLs:	https://www.scopus.com/pages/publication...
Depositing User:	LivePure Connector
Date Deposited:	26 May 2026 12:57
Last Modified:	18 Jun 2026 21:00
URI:	https://ueaeprints.uea.ac.uk/id/eprint/103151
DOI:

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