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

作     者：G.Rezaei Behbehani A.A.Saboury M.Mohebbian S.Tahmasbi Sarvestani M.Poorheravi 

作者机构：Chemistry DepartmentImam Khomeini International UniversityQazvinIran Institute of Biochemistry and BiophysicsUniversity of TehranTehranIran Chemistry DepartmentPayame Noor University(PNU)AbharIran 

出 版 物：《Chinese Chemical Letters》 (中国化学快报（英文版）)

年 卷 期：2009年第20卷第11期

页      面：1389-1392页

核心收录：

学科分类：0710[理学-生物学] 071001[理学-植物学] 07[理学] 

主　　题：Jack bean urease Cyanide ion Isothermal titration calorimetry Binding parameters Inhibitor 

摘      要：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 ofurease, and there is a set of 12 ± 0.12 identical and independent binding sites for CN- ions. The dissociation equilibrium constant is 749.99 umol/L. The molar enthalpy of binding is AH= -13.60 kJ mol^-1.