漆酶与ABTS间的结合模式与作用机制研究  

Binding Mode and Interaction Mechanism of Laccase and ABTS

作　　者：陶国翔[1] 李爱秀[1] 张敏[2] 刘子泉[3] 

机构地区：[1]武警后勤学院基础部药物设计实验室,天津300309 [2]武警后勤学院科研部,天津300309 [3]武警后勤学院附属医院全军灾害应急救援医学重点实验室,天津300162

出　　处：《化学与生物工程》2017年第11期23-26,共4页Chemistry & Bioengineering

基　　金：武警后勤项目(WJHQ2012-14);武警后勤学院重点项目(WHZ201201);武警后勤学院基础研究项目(WHJ2016025);天津市卫生局科技基金项目(2015KZ123)

摘　　要：选择常见的电子转移介质2,2′-连氮基-双(3-乙基-苯并二氢噻唑啉-6-磺酸)(ABTS)为研究对象,通过探究漆酶与ABTS之间的结合模式,在分子水平上揭示两者的相互作用机制,为发掘漆酶新介质、拓宽漆酶应用范围奠定理论基础。首先,基于分子对接建立变色栓菌漆酶-ABTS复合物模型;然后,与枯草芽孢杆菌漆酶-ABTS复合物晶体结构进行对比,综合两复合物结合特点,在分子水平上阐明漆酶与ABTS间的作用机制。结果表明,ABTS结构中的富电子基团深入活性位点,且靠近电子接收位点组氨酸;漆酶活性位点内多个中性氨基酸与ABTS发生疏水作用,稳定结合构象;最终在漆酶作用下ABTS生成阳离子中间体发挥介导作用。In order to find new mediators and provide a theoretical basis for further study on extending the application scope of laccase,we selected the electron transfer mediator--2,2＇-azino-bis（3-ethylbenzthiazoline-6- sulfonic acid）（ABTS） as an object to reveal the binding mode and interaction mechanism at the molecular level between laccase and ABTS. On the basis of molecular docking,we built a complex model of Trametes versicolor laccase-ABTS,and compared the crystal structure of Bacillus subtilis laccase-ABTS complex. Moreover,we ex- plained the interaction mechanism of laccase and ABTS at the molecular level with the binding characteristics of two complexes. The results indicated that the rich electronics group in ABTS penetrated into the laccase active site,and approached the electron acceptor histidine. Many neutral amino acids interacted with ABTS by hydro- phobic interaction at laccase active site,and stablilized the binding conformation. Finally, ABTS turned into cat- ionic intermediate and played a mediated role under the action of laccase.

关 键 词：漆酶 ABTS 漆酶-ABTS体系 分子对接 作用机制 

分 类 号：O641[理学—物理化学]