A thermodynamic study on the binding of mercury and silver ions to urease

被引：12

作者：

Behbehani, G. Rezaei ^{[1
]}

Saboury, A. A. ^{[2
]}

Taherkhani, A. ^{[1
]}

Barzegar, L. ^{[1
]}

Mollaagazade, A. ^{[1
]}

机构：

[1] Islamic Azad Univ, Dept Chem, Fac Sci, Takestan Branch, Takestan, Iran

[2] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

来源：

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY | 2011年 / 105卷 / 03期

关键词：

Jack bean urease; Isothermal titration calorimetry; Inhibitor; Entropy; HIGH-PERFORMANCE METHOD; INHIBITION;

D O I：

10.1007/s10973-011-1729-9

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

In this article, a thermodynamic study on the interaction of Jack bean urease, JBU, with Hg2+ and Ag+ ions were studied by isothermal titration calorimetry (ITC) at 300 and 310 K in 30 mM Tris buffer solution, pH 7.0. The heats of JBU + Hg2+ and JBU + Ag+ interactions are reported and analyzed in terms of the extended solvation model. It was indicated that there are a set of 12 identical and non-cooperative sites for Hg2+ and Ag+ ions. The binding of Hg2+ and Ag+ ions with JBU are exothermic with association equilibrium constants of 5415.65 and 4368.15 for Ag+ and 2389 and 2087M(-1) for Hg2+ at 300 and 310 K, respectively.

引用

页码：1081 / 1086

页数：6

共 14 条

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