血红素
环丙烷化
血红素
化学
催化作用
酶
生物催化
血红素蛋白
组合化学
酶催化
分子动力学
立体化学
反应机理
有机化学
计算化学
作者
Lara Villarino,Kathryn E. Splan,Eswar R. Reddem,Lur Alonso‐Cotchico,Cora Gutiérrez de Souza,Agustı́ Lledós,Jean‐Didier Maréchal,A.M.W.H. Thunnissen,Gérard Roelfes
标识
DOI:10.1002/anie.201802946
摘要
Abstract An artificial heme enzyme was created through self‐assembly from hemin and the lactococcal multidrug resistance regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. However, good catalytic activity and moderate enantioselectivity was observed in an abiological cyclopropanation reaction. We propose that the dynamic nature of the structure of the LmrR protein is key to the observed activity. This was supported by molecular dynamics simulations, which showed transient formation of opened conformations that allow the binding of substrates and the formation of pre‐catalytic structures.
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