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A calorimetric study of the interaction of silver ions with jack bean urease

机译:银离子与杰克豆脲酶相互作用的量热研究

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摘要

A thermodynamic study of silver ions by jack bean urease (JBU) was carried out at 2 temperatures, 27 and 37 °C, in Tris buffer (30 mM; pH 7.0) using isothermal titration calorimetry (ITC). There was a set of 12 identical and noninteracting binding sites for the silver ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding were 185 μM and-16.7 kJ mol~(-1) at 27 ° C, and 229 μM and-16.3 kJ mol~(-1) at 37 °C, respectively. The molar entropy of binding was +15.7 J K~(-1) mol~(-1) at 27 ° C and +17.1 J K~(-1) mol~(-1) at 37 °C. Hence, the binding process of silver ions to JBU is not only enthalpy driven but is also entropy driven, and the role of entropy should be made more effective by increasing the temperature.
机译:使用等温滴定量热法(ITC)在27和37°C的2个温度下,在Tris缓冲液(30 mM; pH 7.0)中,进行了杰克豆脲酶(JBU)对银离子的热力学研究。银离子有一组12个相同且不相互作用的结合位点。本征解离平衡常数和结合摩尔焓在27°C时分别为185μM和-16.7 kJ mol〜(-1),在37°C时分别为229μM和-16.3 kJ mol〜(-1)。结合的摩尔熵在27°C下为+15.7 J K〜(-1)mol〜(-1)在37°C下为+17.1 J K〜(-1)mol〜(-1)。因此,银离子与JBU的结合过程不仅受焓驱动,而且受熵驱动,并且应通过提高温度使熵的作用更有效。

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