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oai:recercat.cat:2072/4552662026-03-13T07:02:45Zcom_2072_98col_2072_378192

00925njm 22002777a 4500 dc Villarino, Lara author Splan, Kathryn E. author Reddem, Eswar author Alonso-Cotchico, Lur author Gutiérrez de Souza, Cora author Lledós, Agustí author Maréchal, Jean-Didier author Thunnissen, Andy-Mark author Roelfes, Gerard author 2018 Altres ajuts: PhD grant from the Generalitat de Catalunya 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. Artificial metalloenzymes Biocatalysis Carbenes Enzyme design Heme enzymes An Artificial Heme Enzyme for Cyclopropanation Reactions