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Investigation of the interactions between indoIe-3-acetic acid and catalase: A spectroscopic study in combination with second-order calibration and molecular docking methods

机译:吲哚-3-乙酸与过氧化氢酶之间相互作用的研究:结合二级校准和分子对接方法的光谱研究

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摘要

The interactions between indole-3-acetic acid (IAA) and the important antioxidant enzyme catalase (CAT) have been studied by Ultraviolet-visible (UV-vis) and fluorescence spectroscopic methods. The decrease of the absorption intensity of CAT at 270 nm and 407 nm in UV-vis spectra with the addition of IAA indicated the interactions between CAT and IAA. The three-way excitation-emission matrix spectra combined with parallel factor analysis (PARAFAC) was used to provide the individual concentration information of IAA, CAT, and IAA-CAT in the reaction system. The PARAFAC analysis showed that a 1 : 1 IAA-CAT complex formed at the equilibrium point. Constant wavelength synchronous fluorescence spectrometry (SFS) showed that the binding of IAA resulted in the micro-environment changes around tryptophan (Trp) and tyrosine (Tyr) residues. Molecular docking studies provide a good structural basis to explain the experimental results. This work is valuable for providing a deeper insight into the interaction mechanism of IAA with CAT.
机译:吲哚-3-乙酸(IAA)与重要的抗氧化酶过氧化氢酶(CAT)之间的相互作用已通过紫外可见(UV-vis)和荧光光谱法进行了研究。加入IAA后,紫外可见光谱中CAT在270 nm和407 nm处的吸收强度降低,表明CAT与IAA之间存在相互作用。三向激发-发射矩阵光谱结合并行因子分析(PARAFAC)用于提供反应系统中IAA,CAT和IAA-CAT的单独浓度信息。 PARAFAC分析表明在平衡点形成了1:1 IAA-CAT复合物。恒定波长同步荧光光谱法(SFS)显示,IAA的结合导致色氨酸(Trp)和酪氨酸(Tyr)残基周围的微环境发生变化。分子对接研究为解释实验结果提供了良好的结构基础。这项工作对于深入了解IAA与CAT的交互机制非常有价值。

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