中文摘要：

细胞色素P450BM3作为烷烃羟基化酶,能催化正链烷烃,已被广发研究和应用。利用动力学模拟软件对BM3酶与烷烃底物复合物进行构象、酶的活性位点以及结合能的预测,并通过模拟水以及离子环境下对复合物的影响,从能量及构象位移的角度阐述BM3酶与底物结合的机理,从而用分子动力学观点来解释细胞色素P450催化烷烃机理。用Autodock等软件将BM3与十六烷对接,发现底物C16与铁原子间距为7.57？,并发现与底物结合的活性位点关键残基：ALA330,ALA74,SER72,GLN73,ALA328,LEU188,LEU437。经Gromacs动力学模拟步长为1ns,温度在298K,压力为常压1.0,复合物结合稳定。

英文摘要：

n-alkane could be catalyzed by monooxygenases cytochrome P450 BM-3 as a n-alkane hydroxylase.Recently,BM3 has been widely engineered on industry application.Complex of ligand and enzyme will be studied by molecular dynamic stimulation method in ions and water environment.It will be discussed from point of energy changed and configuration transformed.Binding energy will be predicted by AUTODOCK 4.0.The mechanism of n-alkane catalyzed by cytochrome P450 will be proposed in molecular dynamic view.As a result,author finds distance of C16（substrate） and iron（heme） to be approximately 7.57 .At the meantime,the key binding active resuide are ALA 330,ALA 74,SER 72,GLN 73,ALA328,LEU 188,and LEU 437.Dynamics analysis by gromacs 4.0.2 for 1 ns show that compound of enzyme and substrate are steady under 1.0 atm and temperature 298 K.