Journal of the Serbian Chemical Society 2013 Volume 78, Issue 2, Pages: 255-263
https://doi.org/10.2298/JSC101005103R
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A calorimetric investigation for the bindings of mushroom tyrosinase to p-phenylene-bis dithiocarbamate and xanthates
Rezaei Behbehani Gholam Reza (Department of Chemistry, Imam Khomeini International University, Qazvin, Iran)
Mehreshtiagh Melisa (Department of Chemistry, Imam Khomeini International University, Qazvin, Iran)
Barzegar Lyla (Department of Chemistry, Islamk Azad University, Takestan branch, Takestan, Iran)
Saboury Akbar Ali (Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran)
A comprehensive, simple and rapid thermodynamic study on the interaction of
Mushroom Tyrosinase, MT, with three iso-alkyldithiocarbonates (xanthates), as
sodium salts, C3H7OCS2Na (I), C4H9OCS2Na (II), C5H11OCS2Na (III) and
p-phenylene-bis dithiocarbamate (IV), by using isothermal titration
calorimetry was carried out to clarify thermodynamics of these bindings as
well as structural changes of the enzyme due to its interaction with
inhibitors at 300K in phosphate buffer (10 m molL-1; pH 6.8).The extended
solvation theory was used to elucidate the effect of the inhibitors on the
stability of enzyme. The obtained results indicate that there are two
identical and non-cooperative binding sites for these inhibitors.
Keywords: mushroom tyrosinase, isopropyl xanthate, isobutyl xanthate, iso-pentyl xanthate, p-phenylene bis(dithiocarbamate), extended solvation theory