Spectroscopic study on the interaction of catalase with bifendate and analogs.
Spectroscopic study on the interaction of catalase with bifendate and analogs.
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DOI：
10.1016/j.saa.2012.10.039
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发表时间：
2013-02
期刊：
影响因子：
--
通讯作者：
Ruiqiang Wang;Lu Zhang;Rui Wang;Huan-jing Dou;Hua Li;Yi Wang;Juanjuan Pu;Ruiyong Wang
中科院分区：
文献类型：
--
作者：
Ruiqiang Wang;Lu Zhang;Rui Wang;Huan-jing Dou;Hua Li;Yi Wang;Juanjuan Pu;Ruiyong Wang
用分光光度法研究了联苯双酯(DDB)及其类似物(双环、I、II、III)与过氧化氢酶的相互作用。荧光光谱结果表明，过氧化氢酶的本征荧光被DDB或类似物用静态猝灭过程强烈猝灭。得到了三种温度下的结合常数。热力学参数(ΔH、ΔS、ΔG)表明疏水作用和静电作用在相互作用中起主要作用。同步荧光、紫外-可见吸收光谱和三维荧光光谱的结果表明，类似物干扰了过氧化氢酶色氨酸残基的微环境。热力学结果表明，在5种化合物中，DDB是最强的猝灭剂，与过氧化氢酶结合的亲和力最高。
The interactions of bifendate (DDB) or analogs (Bicyclol, I, II and III) with catalase are analyzed by spectrophotometric methods. The fluorescence spectra results show the intrinsic fluorescence of catalase is strongly quenched by DDB or analogs with a static quenching procedure. The binding constants are obtained at three temperatures. The thermodynamics parameters (ΔH, ΔS, ΔG) indicate the hydrophobic and electrostatic interactions play a major role in the interaction. The results of synchronous fluorescence, UV–vis absorption and three-dimensional fluorescence spectra demonstrate that the microenvironments of Trp residue of catalase are disturbed by the analogs. Thermodynamic results showed that DDB is the strongest quencher and bind to catalase with the highest affinity among five compounds.