Research on Thermodynamic aspect of the Binding of p-Phenylene-bis dithiocarbamate to Mushroom Tyrosinase

摘要

The binding properties and structural changes of mushroom tyrosinase enzyme, MT, due to its interaction with p-phenylene-bis dithiocarbamate (I) was investigated at 27 and 37-C in phosphate buffer (10 mmol.L~(-1)) at pH 6.8 by isothermal titration calorimetric (ITC). The extended solvation model was used to calculate the solvation parameters, which were attributed to the stability of enzyme. Thermodynamic analysis indicated that the binding of I to MT essentially depends on electrostatic interactions. It was concluded that MT has two distinct sites for p-phenylene-bis and phenyl dithiocarbamate.