Application of a simple calorimetric data analysis on the binding study of cyanide ions by Jack bean urease

被引:7
作者
Behbehani, G. Rezaei [1 ]
Saboury, A. A. [2 ]
Mohebbian, M. [3 ]
Ghammamy, S. [1 ]
机构
[1] Imam Khomeini Int Univ, Dept Chem, Qazvin, Iran
[2] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran
[3] Payame Noor Univ, Dept Chem, Abhar, Iran
关键词
Isothermal titration calorimetry; Cyanide ion; Jack bean urease; Binding parameter; HUMAN GROWTH-HORMONE; ISOTHERMAL TITRATION CALORIMETRY; PRODUCT INHIBITION; CALCIUM-IONS; SPECTROSCOPY;
D O I
10.1016/j.cclet.2009.10.021
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Cyanide ion was studied as an effector of Jack bean urease (JBU) at 300 K in 30 mmol/L Tris buffer, pH 7 by isothermal titration calorimetry (ITC). The simple novel model was used for CN(-) + JBU interaction over the whole range of CN- concentrations. The binding parameters recovered from the simple novel model were attributed to the cyanide ion interaction. It was found that cyanide ion acted as a noncooperative inhibitor of JBU, and there is a set of 12 identical and independent binding sites for CN(-) ions. The dissociation equilibrium constant is 750 mu mol/L. The molar enthalpy of binding is Delta H = -13.6 kJ mol(-1). The technique used provided an accurate and quick assessment of the effectiveness of the compounds to inhibit Jack bean urease. (C) 2009 G. Rezaei Behbehani. Published by Elsevier B.V. on behalf of Chinese Chemical Society. All rights reserved.
引用
收藏
页码:457 / 460
页数:4
相关论文
共 13 条
[1]   Conformational and structural analysis of bovine β lactoglobulin-A upon interaction with Cr+3 [J].
Divsalar, A. ;
Saboury, A. A. ;
Moosavi-Movahedi, A. A. .
PROTEIN JOURNAL, 2006, 25 (02) :157-165
[2]   Structural characteristics of phosphoramide derivatives as urease inhibitors.: Requirements for activity [J].
Font, Maria ;
Dominguez, Maria-Jose ;
Sanmartin, Carmen ;
Palop, Juan A. ;
San-Francisco, Sara ;
Urrutia, Oscar ;
Houdusse, Fabrice ;
Garcia-Mina, Jose M. .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2008, 56 (18) :8451-8460
[3]  
Ghadermarzi M, 1998, POL J CHEM, V72, P2024
[4]   A review on the ligand binding studies by isothermal titration calorimetry [J].
Saboury, A. A. .
JOURNAL OF THE IRANIAN CHEMICAL SOCIETY, 2006, 3 (01) :1-21
[5]   Application of a simple calorimetric data analysis on the binding study of calcium ions by human growth hormone [J].
Saboury, AA ;
Atri, MS ;
Sanati, MH ;
Sadeghi, M .
JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, 2006, 83 (01) :175-179
[6]   A thermodynamic study on the interaction between magnesium ion and human growth hormone [J].
Saboury, AA ;
Atri, MS ;
Sanati, MH ;
Moosavi-Movahedi, AA ;
Hakimelahi, GH ;
Sadeghi, M .
BIOPOLYMERS, 2006, 81 (02) :120-126
[7]   Effects of calcium binding on the structure and stability of human growth hormone [J].
Saboury, AA ;
Atri, MS ;
Sanati, MH ;
Moosavi-Movahedi, AA ;
Haghbeen, K .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2005, 36 (05) :305-309
[8]   Thermodynamic studies on the interaction of calcium ions with alpha-amylase [J].
Saboury, AA ;
Karbassi, F .
THERMOCHIMICA ACTA, 2000, 362 (1-2) :121-129
[9]   New methods for data analysis of isothermal titration calorimetry [J].
Saboury, AA .
JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, 2003, 72 (01) :93-103
[10]   A product inhibition study on adenosine deaminase by spectroscopy and calorimetry [J].
Saboury, AA ;
Divsalar, A ;
Jafari, GA ;
Moosavi-Movahedi, AA ;
Housaindokht, MR ;
Hakimelahi, GH .
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2002, 35 (03) :302-305