中文摘要：

2-巯基噻唑啉是一种被广泛应用的抗腐蚀剂和光亮剂,然而它的一些残留物会对环境造成损坏,为探究2-巯基噻唑啉的毒性作用,采用光谱学技术和分子对接技术来考察2-巯基噻唑啉和过氧化氢酶的相互作用影响,其中酶活性实验表明2-巯基噻唑啉会抑制过氧化氢酶的活性,分子对接结果显示2-巯基噻唑啉会结合在过氧化氢酶的活性位点处,并最终导致过氧化氢酶空间结构和微环境的变化,根据荧光测试结果,表明2-巯基噻唑啉和过氧化氢酶之间的猝灭方式为静态猝灭。通过测量不同温度下的结合位点数、结合常数以及热力学常数,显示2-巯基噻唑啉与过氧化氢酶主要通过氢键和范德华力相结合。该研究从分子水平上考察了2-巯基噻唑啉对蛋白质的毒性作用,对于阐明污染物的毒性机理具有重要意义。

英文摘要：

2-Mercaptothiazoline（2-MT） is a kind of widely used corrosion inhibitor and brightener. The residue of 2-MT in the environment is potentially harmful. To evaluate the toxicity of 2-MT at the protein level,the effects of 2-MT on catalase（ CAT） were investigated by multiple spectroscopic techniques and molecular modeling. The enzyme activity experiment indicated that the CAT activity was inhibited by 2-MT. Molecular docking results revealed that 2-MT bound into the CAT active site,which further led to some secondary structure and micro-environmental changes of CAT. According to the fluorescence results,the quenching mechanism of fluorescence of CAT by 2-MT was a static quenching procedure. The number of binding sites n,the binding constant k and the thermodynamic parameters at different temperatures were also measured. The results indicated that 2-MT can interact with CAT to form a complex mainly by van der Waals＇ interactions and hydrogen bonds. In this paper,we studied the toxic mechanism between 2-mercaptothiazoline and protein at the molecular level,which will conse-quently be significant to learn the toxic effect of pollutants.