Theoretical Study of Iron Porphyrin Imine Specie of P411 Enzyme:Electronic Structure and Regioselectivity of C(sp^(3))-H Primary Amination  

作　　者：LI Shuang WEN Zi-Hao ZHANG Min-Yi 李爽;文子豪;张敏熠(College of Chemistry,Fuzhou University,Fuzhou 350108,China;Fujian Institute of Research on the Structure of Matter,Chinese Academy of Sciences,Fuzhou 350002,China)

机构地区：[1]College of Chemistry,Fuzhou University,Fuzhou 350108,China [2]Fujian Institute of Research on the Structure of Matter,Chinese Academy of Sciences,Fuzhou 350002,China

出　　处：《Chinese Journal of Structural Chemistry》2021年第11期1411-1422,1405,共13页结构化学（英文）

摘　　要：The cytochrome P411 enzyme is a variant of cytochrome P450_(BM3) from Bacillus megaterium whose active site is an iron porphyrin imine([Fe(Por)(NH)]^(-))specie.This specie has been reported to successfully promote the primary amination of benzylic and allylic C(sp^(3))-H bonds.We employed density functional theory to study the electronic structure of the active site of P411 enzyme and the primary amination of C-H bond reaction that it catalyzes.The calculated spin densities and orbital values indicate the existence of resonance in this specie;namely,[(por)(–OH)Fe^(Ⅳ)–N^(2-)–H]^(-)↔[(por)(–OH)Fe^(Ⅲ)–N^(·-)–H]^(-).The amination of C(sp^(3))-H bonds consists of two main reaction steps:hydrogen-atom abstraction and radical recombination,and the former is demonstrated to be the rate-determining step.Furthermore,we studied the regioselectivity of the amination of primary and secondary C(sp^(3))-H bonds.Our calculations indicated that the secondary C(sp^(3))-H bonds of the substrate would be more favored for the activation by P411 enzyme.These results provide valuable information for understanding the properties and selectivity of C-H/C-N bond-activation reactions catalyzed by the P411 enzyme or other similar enzymes.

关 键 词：DFT cytochrome P411 enzyme C-H bond activation enzyme catalysis 

分 类 号：O621.25[理学—有机化学]