Author(s): Rezaei Behbehani Gholam Reza | Mehreshtiagh Melisa | Barzegar Lyla | Saboury Akbar Ali
Journal: Journal of the Serbian Chemical Society
ISSN 0352-5139
Volume: 78;
Issue: 2;
Start page: 255;
Date: 2013;
VIEW PDF
DOWNLOAD PDF 
Original page
Keywords: mushroom tyrosinase | isopropyl xanthate | isobutyl xanthate | iso-pentyl xanthate | p-phenylene bis(dithiocarbamate) | extended solvation theory
ABSTRACT
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.
Journal: Journal of the Serbian Chemical Society
ISSN 0352-5139
Volume: 78;
Issue: 2;
Start page: 255;
Date: 2013;
VIEW PDF
DOWNLOAD PDF Original pageKeywords: mushroom tyrosinase | isopropyl xanthate | isobutyl xanthate | iso-pentyl xanthate | p-phenylene bis(dithiocarbamate) | extended solvation theory
ABSTRACT
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.
