An Artificial Heme Enzyme for Cyclopropanation Reactions

Lara Villarino, Kathryn E. Splan, Eswar Reddem, Lur Alonso-Cotchico, Cora Gutiérrez de Souza, Agustí Lledós, Jean Didier Maréchal, Andy Mark W.H. Thunnissen, Gerard Roelfes

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84 Citations (Scopus)


© 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. 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.
Original languageEnglish
Pages (from-to)7785-7789
JournalAngewandte Chemie - International Edition
Issue number26
Publication statusPublished - 25 Jun 2018


  • artificial metalloenzymes
  • biocatalysis
  • carbenes
  • enzyme design
  • heme enzymes


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