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A Structural and Calorimetric Study on the Interaction Between Jack Bean Urease and Cyanide Ion

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Abstract

The cyanide ion was studied as an effecter of Jack bean urease at 300 K in 30 mmol⋅L−1 Tris buffer, pH=7. The inhibition was investigated by isothermal titration calorimetry (ITC). The extended solvation model was used for CN−+JBU interaction over the whole range of CN− concentrations. The binding parameters recovered from the solvation model were attributed to the interaction with cyanide ion. It was found that cyanide ion acted as a noncooperative inhibitor of urease, and there is a set of 12 identical and independent binding sites for CN− ions. The dissociation equilibrium constant is 749.99 μmol⋅L−1. The molar enthalpy of binding is ΔH=−13.60 kJ⋅mol−1.

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Authors and Affiliations

  1. Chemistry Department, Imam Khomeini International University, Qazvin, Iran

    Gholamreza Rezaei Behbehani

  2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    Ali A. Saboury

  3. Chemistry Department, Payame Noor University (PNU), Abhar, Iran

    Maryam Mohebbian, Sanaz Tahmasebi & Mohammadfeza Poorheravi

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  1. Gholamreza Rezaei Behbehani
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  2. Ali A. Saboury
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  3. Maryam Mohebbian
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  4. Sanaz Tahmasebi
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  5. Mohammadfeza Poorheravi
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Correspondence to Gholamreza Rezaei Behbehani.

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Rezaei Behbehani, G., Saboury, A.A., Mohebbian, M. et al. A Structural and Calorimetric Study on the Interaction Between Jack Bean Urease and Cyanide Ion. J Solution Chem 38, 1612–1621 (2009). https://doi.org/10.1007/s10953-009-9471-7

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  • DOI: https://doi.org/10.1007/s10953-009-9471-7

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