| 百草枯与牛血清白蛋白结合作用的荧光光谱 |
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| 引用本文： | 颜承农,张华新,刘义,梅平,李克华,童金强.百草枯与牛血清白蛋白结合作用的荧光光谱[J].化学学报,2005,63(18):1727-1732. |
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| 作者姓名： | 颜承农 张华新 刘义 梅平 李克华 童金强 |
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| 作者单位： | (1长江大学化学与环境工程学院 荆州 434020)(2武汉大学化学与分子科学学院 武汉 430072) |
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| 基金项目： | 国家自然科学基金（No.30170010）、湖北省教育厅重点（No.2003A003）和湖北省自然科学基金（No.2005ABA067）资助项目. |
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| 摘 要： | 在模拟动物体生理条件下, 用荧光光谱和紫外-可见吸收光谱法研究了在不同温度下, 百草枯(PQ)与牛血清白蛋白(BSA)结合反应的光谱行为. 试验发现, PQ对BSA有较强的荧光猝灭作用. 用Stern-Volmer和Lineweaver-Burk方程分别处理试验数据, 发现BSA与PQ发生反应生成了新的复合物, 属于静态荧光猝灭, 发生分子内的非辐射能量转移. 根据F?rster的偶极-偶极非辐射能量转移理论计算出结合位置距离212位色氨酸残基2.07 nm. 由Lineweaver-Burk方程求出了不同温度下反应时复合物的形成常数KLB (297 K: 2.035×104 L•mol－1; 304 K: 3.256×104 L•mo－1; 311 K: 2.889×104 L•mol－1)及对应温度下结合反应的热力学参数(⊿HØ＝18.50 kJ•mol－1;⊿SØ＝144.7 J•K－1/145.2 J•K－1/141.0 J•K－1; ⊿GØ＝－24.50 kJ•mol－1/－25.66 kJ•mol－1/－25.36 kJ•mol－1), 证明二者主要靠疏水作用力结合. 同时用三维荧光光谱及同步荧光光谱法探讨了PQ对BSA构象的影响, 为预防和医治PQ中毒提供了重要依据.
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| 关 键 词： | 百草枯 牛血清白蛋白 结合反应 热力学参数 吸收光谱 三维荧光光谱 |
| 收稿时间： | 2004-12-27 |
| 修稿时间： | 2005-5-20 |
Fluorescence Spectra of the Binding Reaction between Paraquat and Bovine Serum Albumin |
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| YAN Cheng-nong,ZHANG Hua-xin,LIU Yi,Mei Ping,LI Ke-hua,TONG Jin-qiang.Fluorescence Spectra of the Binding Reaction between Paraquat and Bovine Serum Albumin[J].Acta Chimica Sinica,2005,63(18):1727-1732. |
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| Authors: | YAN Cheng-nong ZHANG Hua-xin LIU Yi Mei Ping LI Ke-hua TONG Jin-qiang |
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| Affiliation: | (1 College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou 434020)(2 College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072) |
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| Abstract: | Under the imitated physiological condition of animal body, the binding of paraquat to bovine serum albumin (BSA) was studied by fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence launching from BSA. After analyzing the fluorescence quenching data according to Stern-Volmer equation and Lineweaver-Burk double-reciprocal equation, we found that BSA had reacted with paraquat and formed a certain new compound. The quenching belonged to static fluorescence quenching, with non-radiation energy transfer happening within single molecule. The binding locality was an area 2.07 nm away from tryptophan residue-212 in BSA based on F?rster’s non-radiation energy transfer mechanism. According to Lineweaver-Burk equation, KLB (297 K: 2.035×104 L•mol－1; 304 K: 3.256×104 L•mo－1; 311 K: 2.889×104 L•mol－1), the forming constants of the compound at different temperatures and the thermodynamic parameters (⊿HØ＝18.50 kJ•mol－1; ⊿SØ＝144.7 J•K－1/145.2 J•K－1/141.0 J•K－1; ⊿GØ＝－24.50 kJ•mol－1/－25.66 kJ•mol－1/－25.36 kJ•mol－1) at correspondence temperatures were obtained. The latter shows that binding power between them is mainly the hydrophobic interaction. The effect of paraquat on the conformation of BSA was analyzed by three-dimensional fluorescence spectra, contour spectra and synchronous spectra, and some useful information was offered for preventing animals from infecting paraquat and curing those who had caught it. |
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| Keywords: | paraquat bovine serum albumin binding reaction thermodynamic parameter absorption spectra three-dimensional fluorescence spectra |
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