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Thermal investigation of the interaction between Phenyl Dithiocarbamate and mushroom tyrosinase

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Author Affiliations

  • 1Department of Chemistry, faculty of science, Islamic azad university, Takestan branch, Takestan, IRAN
  • 2Institute of Biochemistry and Biophysics, University of Tehran, Tehran, IRAN

Res.J.chem.sci., Volume 2, Issue (3), Pages 68-70, March,18 (2012)

Abstract

A comprehensive, simple and rapid thermodynamic study on the interaction of Mushroom Tyrosinase (MT) with Phenyl Dithiocarbamate by using isothermal titration calorimetry at 27 and 37°C in phosphate buffer (10 mM) at pH 6.8, was carried out to see whether Phenyl Dithiocarbamate induced conformational change of Mushroom Tyrosinase and how changes by ligand binding were occurred. The extended solvation theory can be used to elucidate the stability of enzyme by Phenyl Dithiocarbamate. The negative change of the Gibbs free energy at two temperatures of 27 and 37°C shows that the binding process in both temperatures are spontaneous. The obtained results indicate that there are two identical and non-cooperative binding sites for Phenyl dithiocarbamate.

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