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

In this article, a thermodynamic study on the interaction of Jack bean urease, JBU, with and 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 and interactions are reported and analyzed in terms of the extended solvation...

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Veröffentlicht in:	Journal of thermal analysis and calorimetry 2011-09, Vol.105 (3), p.1081-1086
Hauptverfasser:	Rezaei Behbehani, G., Saboury, A. A., Taherkhani, A., Barzegar, L., Mollaagazade, A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analysis Analytical Chemistry Binding Biological and medical sciences Buffer solutions Calorimetry Chemical properties Chemistry Chemistry and Materials Science Enzymes Fundamental and applied biological sciences. Psychology Hydrolases Inorganic Chemistry Interactions. Associations Intermolecular phenomena Jack beans Measurement Science and Instrumentation Mercury Molecular biophysics Physical Chemistry Polymer Sciences Solvation Thermal properties Thermodynamics Titration calorimetry
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Beschreibung
Zusammenfassung:	In this article, a thermodynamic study on the interaction of Jack bean urease, JBU, with and 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 and 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 and ions. The binding of and ions with JBU are exothermic with association equilibrium constants of 5415.65 and 4368.15 for and 2389 and 2087 for at 300 and 310 K, respectively.
ISSN:	1388-6150 1588-2926 1572-8943
DOI:	10.1007/s10973-011-1729-9