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Calorimetric studies of the interaction of myosin with ADP.

A calorimetric titration method was used to study ADP binding to native myosin. Data were analyzed by assuming that the myosin molecule has n independent and identical sites for ADP binding. The enthalpy change (deltaH), the binding constant (K), and n were determined. In 0.5 M KCl, 0.01 M MgCl2, and 0.02 M Tris/HCl (pH 7.8), we found: at 0 degrees, deltaH = -57.1 +/- 3.2 kJ-mol-1, log K = 6.42 +/- 0.13, n = 1.49 +/- 0.07; at 12 degrees, deltaH = 73.1 +/- 3.2 kJ-mole-1, log K = 6.08 +/- 0.13, and n = 1.74 +/- 0.07. The average heat capacity change on ADP binding to myosin between 0 and 12 degrees is thus -1.4 +/- 0.4 kJ-mol-1-K-1. Reasonably consistent results were obtained at 25 degrees, suggesting ADP binding to myosin is as strongly exothermic as at lower temperatures, although further interpretation of this result seems unwarranted, mainly because of the instability of myosic at this temperature. The number of protons released on binding of ADP to myosin was determined in separate experiments. The value was 0.19 +/- 0.02 at both 0 and 12 degrees. The reaction of protons with Tris thus contributes about -9.5 kJ-mol-1 to the observed heat on ADP binding.