荧光光谱法研究除草剂扑草净和扑灭通与过氧化氢酶的相互作用  

Interaction between Triazine Herbicide and Catalase by Fluorescence Spectrum

作　　者：刘维屏[1] 杨炜春[1] 刘惠君[1] 童裳伦[1] 方兆华[1] 

机构地区：[1]浙江大学环境科学研究所,浙江杭州310027

出　　处：《光谱学与光谱分析》2003年第5期926-929,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金(批准号:39670420)资助

摘　　要：应用荧光光谱法研究了水溶液中三嗪类除草剂扑草净和扑灭通与过氧化氢酶分子间的相互作用.结果表明,除草剂对过氧化氢酶的荧光均有较强的猝灭作用,且静态猝灭是引起CAT荧光猝灭的主要原因.从荧光猝灭结果求出除草剂和CAT的结合常数及结合位点数.扑灭通:K=6.17×106 L·mol-1, n=1.45;扑草净:K= 2.12×105 L·mol-1, n=1.19.并依据能量转移机制,求出了扑灭通、扑草净和CAT相互结合时,其给体-受体间距离r分别为0.140和0.155 nm.由此可见,扑灭通与CAT的结合作用要强于扑草净,并推测出除草剂与CAT的Tyr214发生结合作用.The binding of triazine herbicide to catalase in aqueous solution was studied using fluorescence spectroscopy. It was shown that the herbicide has a strong ability to quench the CAT fluorescence mainly through a static quenching procedure. The binding constant K and the number of binding site n were calculated according to the fluorescence quenching results. For prometryn, K = 6.17 X 10(6) L.mol(-1) and n was 1.45; for prometon, K = 2.12 X 10(6) L.mol(-1) and n was 1.19. Based on the mechanism of energy transfer, the distances between acceptor herbicide and CAT were obtained. The distances are r (prometryn) = 0.140 nm and r (prometon) = 0.155 nm. It is clear that the binding of prometryn with catalase is stronger than that of prometon. It is inferred that the binding site between herbicides and catalase was Tyr-214.

关 键 词：荧光光谱法 除草剂 扑草净 扑灭通 过氧化氢酶 

分 类 号：TQ457.2[化学工程—农药化工] O657.34[理学—分析化学]