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Thermodynamic study on the interaction of Co2+ with Jack bean urease

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Author(s): Lyla Barzegar | Gholamreza Rezaei Behbehani | Mohammad Mirzaie | Ali Taherkhani

Journal: Current Chemistry Letters
ISSN 1927-7296

Volume: 1;
Issue: 1;
Start page: 41;
Date: 2012;
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Keywords: Isothermal Titration Calorimetry | Jack bean urease | Cobalt ion

ABSTRACT
The interaction of Jack Bean Urease with cobalt (II) ion was studied by Isothermal Titration Calorimetry (ITC) at 300 K and 310 K in 30 mM Tris buffer, pH=7. The stability of the enzyme increases due to its binding with cobalt ions. The extended solvation model was used to reproduce the heats of Co2++JBU interaction. It was found that there is a set of 12 equivalent and noninteracting binding sites for Co2+ ions. The association equilibrium constant and the molar enthalpy of binding are 4260.76M-1, -16.5 kJmol-1 at 300 K and 3438M-1, -16 kJmol-1 at 310 K, respectively.

Tango Jona
Tangokurs Rapperswil-Jona

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