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Thermodynamic study on the interaction of Co2 with Jack Bean Urease

Author Affiliations

  • 1Chemistry Department, Islamic Azad University, Takestan branch, Takestan, IRAN

Res.J.chem.sci., Volume 2, Issue (6), Pages 88-90, June,18 (2012)

Abstract

The interaction of Jack Bean Urease(IBU) with cobalt (II) ion was studied by isothermal titration calorimetry (ITC) at 300 Kand 310 K in 30 mM Tris buffer, pH=7. The stability of the enzyme increases due to its binding with cobalt ions. The extended solvation model was used to reproduce the heats of Co2++JBU interaction. It was found that there is a set of 12 equivalent and non-interacting binding sites for Co2+ ions. The association equilibrium constant and the molar enthalpy of binding are4260.76M-1 -16.5 kJmol-1at 300 K and 3438M-1, -16 kJmol-1at 310 K, respectively.

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