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- W2079069871 abstract "Xanthine oxidase (XO) and copper, zinc superoxide dismutase (Cu, Zn-SOD) are function-related proteins in vivo. Thermodynamics of the interaction of bovine milk XO with bovine erythrocyte Cu, Zn-SOD has been studied using isothermal titration calorimetry (ITC) and fluorescence spectroscopy. The binding of XO to Cu, Zn-SOD is driven by a large favorable enthalpy decrease with a large unfavorable entropy reduction, and shows strong entropy–enthalpy compensation and weak temperature-dependence of Gibbs free energy change. An unexpected, large positive molar heat capacity change of the binding, 3.02 kJ mol−1 K−1, at all temperatures examined suggests that either hydrogen bond or long-range electrostatic interaction is a major force for the binding. XO quenches the intrinsic fluorescence of Cu, Zn-SOD and causes a small red shift in the fluorescence emission maximum of the protein. A small salt concentration dependence of the binding affinity measured by fluorescence spectroscopy and a large unfavorable change in entropy for the binding measured by ITC suggest that long-range electrostatic forces do not play an important role in the binding. These results indicate that XO binds to Cu, Zn-SOD with high affinity and that hydrogen bond is a major force for the binding." @default.
- W2079069871 created "2016-06-24" @default.
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- W2079069871 date "2005-02-01" @default.
- W2079069871 modified "2023-09-23" @default.
- W2079069871 title "Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase studied by isothermal titration calorimetry and fluorescence spectroscopy" @default.
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- W2079069871 doi "https://doi.org/10.1016/j.tca.2004.07.018" @default.
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