An Artificial Heme Enzyme for Cyclopropanation Reactions

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

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

50 Citaten (Scopus)
336 Downloads (Pure)


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.

Originele taal-2English
Pagina's (van-tot)7785-7789
Aantal pagina's5
TijdschriftAngewandte Chemie - International Edition
Nummer van het tijdschrift26
Vroegere onlinedatum2018
StatusPublished - 25-jun-2018

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