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

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Author Affiliations

  • 1Chemistry Department, Imam Khomeini International University, Qazvin, IRAN
  • 2Department of Chemistry, Faculty of Science, Islamic Azad University, Takestan Branch, Takestan, IRAN

Res.J.chem.sci., Volume 2, Issue (3), Pages 71-73, March,18 (2012)

Abstract

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 37C 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.

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