Application of the extended solvation model for thermodynamic study of copper ion binding to Jack bean urease |
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| Authors: | G Rezaei Behbehani A A Saboury E Poorakbar L Barzegar |
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| Institution: | (1) Chemistry Department, Imam Khomeini International University, Qazvin, Iran;(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Islamic Republic of Iran;(3) Biology Department, Payam Noor University, Tehran, Islamic Republic of Iran |
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| Abstract: | A Thermodynamic study on the interaction Jack bean urease, JBU, with Cu2+ ion was studied by isothermal titration calorimetry (ITC) at 300 and 310 K in 30 mM Tris buffer solution, pH 7.0. The heats
of JBU + Cu2+ interactions are reported and analyzed in terms of the extended solvation theory. It was indicated that there are a set of
12 identical and non-cooperative sites for Cu2+ ion. The binding of Cu2+ ion with JBU is exothermic with dissociation equilibrium constants of 284.883 and 345.855 μM at 300 and 310 K, respectively. |
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