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New methods for Data Analysis of Isothermal Titration Calorimetry for studying binding of two n-alkyl Xanthates to Mushroom Tyrosinase

Author Affiliations

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

Res.J.chem.sci., Volume 2, Issue (4), Pages 76-78, April,18 (2012)

Abstract

A simple rapid direct isothermal titration calorimetry (ITC) method was applied to study the binding properties and structural changes of mushroom tyrosinase enzyme (MT) due to the interaction with two iso-alkyl dithiocarbonates (xanthates), C3H7OCS2Na (I) and C4H9OCS2Na (II) at 27 C in phosphate buffer (10 mM) at pH 6.8. The extended solvation model provides more insights into this interaction for further understanding of the effect of iso-propyl and iso-butyl xanthate on the stability and the structural changes of MT. The solvation parameters derived from the solvation model can be related to the changes in the stability of enzyme and type of inhibition. ITC implies that there is a set of two binding sites for two new synthesized xanthates on MT with non cooperativity in the binding process.

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