Citation: G. Rezaei Behbehani, A. A. Saboury, M. Mohebbian, S. Tahmasbi Sarvestani, M. Poorheravi. Thermodynamic study of CN^-ion inhibition of Jack bean urease using the extended solvation theory[J]. Chinese Chemical Letters, ;2009, 20(11): 1389-1392. doi: 10.1016/j.cclet.2009.05.029 shu

Thermodynamic study of CN^-ion inhibition of Jack bean urease using the extended solvation theory

a Chemistry Department, Imam Khomeini International University, Qazvin, Iran;
b Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;
c Chemistry Department, Payame Noor University (PNU), Abhar, Iran

Received Date: 18 March 2009

Cyanide ion was studied as an inhibitor of Jack bean urease at 300 K in 30 mmol/L tris buffer, pH 7. The inhibition was investigated by isothermal titration calorimetry (ITC). The extended solvation model was used for CN ^-+ JBU interaction over the whole range of CN^-concentrations. The binding parameters recovered from the solvation model were attributed to the cyanide ion interaction. It was found that cyanide ion acted as a non-cooperative inhibitor of urease, and there is a set of 12±0.12 identical and independent binding sites for CN^- ions. The dissociation equilibrium constant is 749.99 mmol/L. The molar enthalpy of binding is △H=-13.60 kJ mol^-1.
- Jack bean urease,
- Cyanide ion,
- Isothermal titration calorimetry,
- Binding parameters,
- Inhibitor
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