Open AccessA calorimetric investigation for the bindings of mushroom tyrosinase to p-phenylene-bis dithiocarbamate and xanthates
Author(s) -
Behbehani Gholam Reza Rezaei,
Melisa Mehreshtiagh,
L. Barzegar,
Akbar Ali Saboury
Publication year - 2013
Publication title -
journal of the serbian chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.227
H-Index - 45
eISSN - 1820-7421
pISSN - 0352-5139
DOI - 10.2298/jsc101005103r
Subject(s) - isothermal titration calorimetry , dithiocarbamate , chemistry , solvation , titration , phenylene , calorimetry , enzyme , tyrosinase , inorganic chemistry , nuclear chemistry , organic chemistry , molecule , thermodynamics , physics , polymer
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