Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1258022 | Chinese Chemical Letters | 2009 | 4 Pages |
Abstract
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 CNâ + JBU interaction over the whole range of CNâ 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 CNâ ions. The dissociation equilibrium constant is 749.99 μmol/L. The molar enthalpy of binding is ÎH = â13.60 kJ molâ1.
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Authors
G. Rezaei Behbehani, A.A. Saboury, M. Mohebbian, S. Tahmasbi Sarvestani, M. Poorheravi,