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Thermal Investigation of three n-alkyl Xanthates binding with Mushroom Tyrosinase

Author Affiliations

  • 1Department of Chemistry, Imam Khomeini International University, Qazvin, IRAN
  • 2Department of Chemistry, Faculty of science, Islamic Azad University, Takestan branch, Takestan, IRAN
  • 3Institute of Biochemistry and Biophysics, University of Tehran, Tehran, IRAN

Res.J.chem.sci., Volume 2, Issue (5), Pages 81-84, May,18 (2012)

Abstract

The interaction between three iso-alkyldithiocarbonates (xanthates), as sodium salts, C3H7OCS2Na (I), C4H9OCS2Na (II), C5H11OCS2Na (III) and mushroom tyrosinase enzyme, MT, have been investigated by isothermal titration calorimetry to clarify thermodynamics of these bindings as well as structural changes of the enzyme due to its interaction with xanthates at 27C in phosphate buffer (10 mmol.L-1; pH=6.8). The extended solvation model was used to elucidate the effect of these xanthates on the stability of the enzye. The values of δA and δB were attributed to the type of inhibition for I, II and III. The obtained results indicate that there are two identical and non-cooperative binding sites for three xanthates.

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