A Structural and Calorimetric Study on the Interaction Between Jack Bean Urease and Cyanide Ion

作者：Behbehani Gholamreza Rezaei^*; Saboury Ali A; Mohebbian Maryam; Tahmasebi Sanaz; Poorheravi Mohammadfeza

来源：Journal of Solution Chemistry, 2009, 38(12): 1612-1621.

DOI：10.1007/s10953-009-9471-7

• Jack bean urease
• Cyanide ion
• Isothermal titration calorimetry
• Binding parameters
• Inhibitor

The cyanide ion was studied as an effecter of Jack bean urease at 300 K in 30 mmola <...L(-1) 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 interaction with cyanide ion. It was found that cyanide ion acted as a noncooperative inhibitor of urease, and there is a set of 12 identical and independent binding sites for CN(-) ions. The dissociation equilibrium constant is 749.99 mu mola <...L(-1). The molar enthalpy of binding is Delta H=-13.60 kJa <...mol(-1).

• 出版日期2009-12