Application of the extended solvation model for thermodynamic study of copper ion binding to Jack bean urease

Behbehani, G. Rezaei; Saboury, Ali Akbar; Poorakbar, Elahe; Barzegar, L.

doi:10.1007/s10973-010-0842-5

Cited by 4 publications

(5 citation statements)

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“…Protein interactions with small ligands (including co‐factors and drugs) Protein/peptide interactions with metals and ions Protein/peptide interactions with nucleic acids …”

Section: Introductionmentioning

confidence: 99%

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Ghai

Falconer

Collins

2011

J of Molecular Recognition

165

108

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Isothermal titration calorimetry (ITC) is a biophysical technique for measuring the formation and dissociation of molecular complexes and has become an invaluable tool in many branches of science from cell biology to food chemistry. By measuring the heat absorbed or released during bond formation, ITC provides accurate, rapid, and label-free measurement of the thermodynamics of molecular interactions. In this review, we survey the recent literature reporting the use of ITC and have highlighted a number of interesting studies that provide a flavour of the diverse systems to which ITC can be applied. These include measurements of protein-protein and protein-membrane interactions required for macromolecular assembly, analysis of enzyme kinetics, experimental validation of molecular dynamics simulations, and even in manufacturing applications such as food science. Some highlights include studies of the biological complex formed by Staphylococcus aureus enterotoxin C3 and the murine T-cell receptor, the mechanism of membrane association of the Parkinson's disease-associated protein α-synuclein, and the role of non-specific tannin-protein interactions in the quality of different beverages. Recent developments in automation are overcoming limitations on throughput imposed by previous manual procedures and promise to greatly extend usefulness of ITC in the future. We also attempt to impart some practical advice for getting the most out of ITC data for those researchers less familiar with the method.

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“…Protein interactions with small ligands (including co‐factors and drugs) Protein/peptide interactions with metals and ions Protein/peptide interactions with nucleic acids …”

Section: Introductionmentioning

confidence: 99%

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Ghai

Falconer

Collins

2011

J of Molecular Recognition

165

108

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“…We have shown previously that the heats of the ligand + HSA interactions in the aqueous solvent mixtures, can be calculated via the following equation [9][10][11][12][13][14]:…”

Section: Resultsmentioning

confidence: 99%

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

Behbehani

Sadr

Nabipur

et al. 2013

Journal of Chemistry

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Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106and 3.86105 M−1for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide.

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“…This investigation is the first of its kind performed for these systems. Earlier, only prefatory results on the thermodynamics of urease inhibition by heavy metal ions were reported in this journal [68,69]. In this present work, the thermodynamics of the binding of the chosen inhibitors to the enzyme is comprehensively studied, interpreted in terms of their affinity to the enzyme and compared with the binding of the substrate.…”

Section: Competitive Inhibitionmentioning

confidence: 91%

“…and Cd 2? ions, measured with use of isothermal titration calorimetry [68][69][70]. Importantly, unlike the competitive inhibitors in this work, heavy metal ions are comparatively strong inhibitors of urease, strongest being Hg 2?…”

Section: Effect Of Temperature On K Imentioning

confidence: 98%

“…The inhibitory action of the ions was proven to be primarily through the reaction with the enzyme thiol groups [46]. Intriguingly, the reported thermodynamic parameters for the binding of the ions to urease [68][69][70] do not vary among the ions, maintaining practically the same values irrespective of the ions' inhibitory strength. The reported values are: DH°& -14 kJ mol -1 (between -16 and -13 kJ mol -1 ), DS°& 19 J K -1 mol -1 (between 17 and 20 J K -1 mol -1 ), DG 300 & -20 kJ mol -1 (between -21 and -20 kJ mol -1 ).…”

Section: Effect Of Temperature On K Imentioning

confidence: 99%

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Thermodynamic study of competitive inhibitors’ binding to urease

Krajewska

Brindell

2015

J Therm Anal Calorim

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Three competitive inhibitors of urease: boric acid, 2-mercaptoethanol and phosphate buffer pH 6.45, were subjected to the studies of temperature effects on their binding to the enzyme. The first of their kind for these systems, the studies were carried out at temperatures between 15 and 35°C in HEPES buffers. The Michaelis K M and inhibition K i constants determined for the uninhibited and inhibited urease reactions, respectively, were found to increase with an increase in temperature, importantly, the inhibition remaining competitive irrespective of temperature. The inverse of the constants were further analyzed as equilibrium constants of substrate and inhibitor binding reactions resulting in the formation of ES and EI complexes. The reactions were thermodynamically analyzed with use of the van't Hoff equation. Found pH-independent in the pH range 6.45-7.0, the changes in the standard enthalpy (DH°= -14 kJ mol -1 ) and the Gibbs free energy (DG 298 = -14 kJ mol -1 ) for the substrate binding were negative, proving favorable for an exothermic and spontaneous reaction. With the standard entropy change DS°close to zero, the reaction is enthalpy driven. The thermodynamic functions of the inhibitor binding by contrast, were found strongly correlated with the inhibitory strengths of the inhibitors in the order: boric acid [ 2-mercaptoethanol [ phosphate buffer pH 6.45. Accordingly, boric acid demonstrated the changes in the thermodynamic functions considerably bigger (DH°= -42 kJ mol -1 , DG 298 = -23 kJ mol -1 ) than the substrate and the other two inhibitors. Those for 2-mercaptoethanol were DH°= -20 kJ mol -1 and DG 298 = -17 kJ mol -1 , while for phosphate buffer pH 6.45, DH°= -17 kJ mol -1 , and DG 298 = -13 kJ mol -1 , and although slightly bigger, they were found practically comparable in value with those of the substrate, features that apparently result from the comparable values of K M and K i s. Remarkably, the inhibitors showed negative values of DS°(to various degrees) proving that their binding to the enzyme, like that of the substrate, is driven by enthalpy.

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Application of the extended solvation model for thermodynamic study of copper ion binding to Jack bean urease

Cited by 4 publications

References 20 publications

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

Thermodynamic study of competitive inhibitors’ binding to urease

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