Thermodynamic study on the interaction of Co2+ with Jack bean urease
| Autor: | Gholamreza Rezaei Behbehani, Lyla Barzegar, Mohammad Mirzaie, Ali Taherkhani |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: | |
| Zdroj: | Current Chemistry Letters, Vol 1, Iss 1, Pp 41-46 (2012) |
| Druh dokumentu: | article |
| ISSN: | 1927-7296 1927-730X |
| Popis: | 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. |
| Databáze: | Directory of Open Access Journals |
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