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, 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

Full text not available from this repository.

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:	31 May 2026 05:28
URI:	https://ueaeprints.uea.ac.uk/id/eprint/103151
DOI:

Actions (login required)

View Item