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

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

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...

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Main Authors: Gholamreza Rezaei Behbehani, Lyla Barzegar, Mohammad Mirzaie, Ali Taherkhani
Format: Article
Language:English
Published: Growing Science 2012-01-01
Series:Current Chemistry Letters
Subjects:
Isothermal Titration Calorimetry
Jack bean urease
Cobalt ion
Online Access:http://www.growingscience.com/ccl/Vol1/ccl_2012_6.pdf
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spelling doaj-d101e8fad9a541d18e52b2fff25a7ff92020-11-24T21:08:50ZengGrowing ScienceCurrent Chemistry Letters1927-72961927-730X2012-01-01114146Thermodynamic study on the interaction of Co2+ with Jack bean urease Gholamreza Rezaei BehbehaniLyla BarzegarMohammad MirzaieAli TaherkhaniThe 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.http://www.growingscience.com/ccl/Vol1/ccl_2012_6.pdfIsothermal Titration CalorimetryJack bean ureaseCobalt ion
collection DOAJ
language English
format Article
sources DOAJ
author Gholamreza Rezaei Behbehani
Lyla Barzegar
Mohammad Mirzaie
Ali Taherkhani
spellingShingle Gholamreza Rezaei Behbehani
Lyla Barzegar
Mohammad Mirzaie
Ali Taherkhani
Thermodynamic study on the interaction of Co2+ with Jack bean urease
Current Chemistry Letters
Isothermal Titration Calorimetry
Jack bean urease
Cobalt ion
author_facet Gholamreza Rezaei Behbehani
Lyla Barzegar
Mohammad Mirzaie
Ali Taherkhani
author_sort Gholamreza Rezaei Behbehani
title Thermodynamic study on the interaction of Co2+ with Jack bean urease
title_short Thermodynamic study on the interaction of Co2+ with Jack bean urease
title_full Thermodynamic study on the interaction of Co2+ with Jack bean urease
title_fullStr Thermodynamic study on the interaction of Co2+ with Jack bean urease
title_full_unstemmed Thermodynamic study on the interaction of Co2+ with Jack bean urease
title_sort thermodynamic study on the interaction of co2+ with jack bean urease
publisher Growing Science
series Current Chemistry Letters
issn 1927-7296
1927-730X
publishDate 2012-01-01
description 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.
topic Isothermal Titration Calorimetry
Jack bean urease
Cobalt ion
url http://www.growingscience.com/ccl/Vol1/ccl_2012_6.pdf
work_keys_str_mv AT gholamrezarezaeibehbehani thermodynamicstudyontheinteractionofco2withjackbeanurease
AT lylabarzegar thermodynamicstudyontheinteractionofco2withjackbeanurease
AT mohammadmirzaie thermodynamicstudyontheinteractionofco2withjackbeanurease
AT alitaherkhani thermodynamicstudyontheinteractionofco2withjackbeanurease
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