Enthalpy of nucleotides binding to myosin

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Abstract
The enthalpies of binding ADP and 5''-adenylyl imidodiphosphate [AMP-P(NH)P] to rabbit skeletal myosin were measured in Pipes and Tris buffers at pH 7.8 and 15.degree. C. For ADP the enthalpy of binding was exothermic, whereas the enthalpy of binding AMP-P(NH)P, a nonhydrolyzable ATP analogue, was small and endothermic. For the reaction of ATP and myosin, the development of enthalpy was resolved into 2 phases: a fast endothermic phase, which is the summation of binding and hydrolysis, and a slow exothermic phase, which is associated with product-release steps. These results are discussed in terms of their implications for energy transduction.

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