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利用紫外吸收光谱法和荧光光谱法研究了异烟肼(NH)与铜锌超氧化物歧化酶(Cu-ZnSOD)的结合作用。结果表明,NH与Cu-ZnSOD的结合行为使Cu-ZnSOD的内源荧光猝灭。通过猝灭常数、结合常数和结合位点的计算,证明荧光猝灭机理符合静态机制;NH和Cu-ZnSOD形成了1∶1稳定复合物,且复合物的形成不影响酶的活力。NH本身具有一定的超氧负离子清除能力。考察不同温度下的猝灭作用,进一步证实结合作用主要受范德华力和氢键驱动。
The binding of isoniazid (NH) to copper-zinc superoxide dismutase (Cu-ZnSOD) was studied by ultraviolet absorption spectroscopy and fluorescence spectroscopy. The results showed that the binding of NH and Cu-ZnSOD quenched the endogenous fluorescence of Cu-ZnSOD. The quenching constants, binding constants and binding sites were calculated to show that the fluorescence quenching mechanism was consistent with the static mechanism. NH and Cu-ZnSOD formed a 1: 1 stable complex, and the complex formation did not affect the enzyme activity. NH itself has some superoxide anion scavenging ability. The quenching effect at different temperatures was investigated, further confirming that the binding was mainly driven by van der Waals forces and hydrogen bonding.