Academic Journals Database
Disseminating quality controlled scientific knowledge

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

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;
VIEW PDF   PDF DOWNLOAD PDF   Download PDF Original page

Keywords: Isothermal Titration Calorimetry | Jack bean urease | Cobalt ion

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

     Save time & money - Smart Internet Solutions