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Biophysical Journal 54: 97-104 (1988)
© 1988 the Biophysical Society

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Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells.

R C Woledge and P J Reilly

Department of Physiology, University College London, United, Kingdom.

ABSTRACT

The enthalpy change for the hydrolysis of phosphorylcreatine (PCr) by hydrochloric acid or by alkaline phosphatase was observed at 0, 25, and 37 degrees C. The value for delta H is -44 kJ mol-1 under alkaline, Mg2+-free conditions and is almost independent of temperature, ionic strength, and concentration of reactants. In muscle the reaction is accompanied by a transfer of protons from the buffers (largely histidine) to orthophosphate, release of Mg2+ from PCr, and binding of Mg2+ to orthophosphate. Measurements are reported of the heats of these processes. The calculated value of the overall heat of hydrolysis of PCr (including these processes) at pH 7, pMg 3 is -35 kJ mol-1.




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