An Artificial Heme Enzyme for Cyclopropanation Reactions

DOI Web Site Web Site 被引用文献8件
  • Lara Villarino
    Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
  • Kathryn E. Splan
    Department of Chemistry Macalester College 1600 Grand Avenue Saint Paul MN 55105 USA
  • Eswar Reddem
    Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
  • Lur Alonso‐Cotchico
    Departament de Química Universitat Autònoma de Barcelona Edifici C.n. 08193 Cerdanyola del Vallés Barcelona Spain
  • Cora Gutiérrez de Souza
    Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
  • Agustí Lledós
    Departament de Química Universitat Autònoma de Barcelona Edifici C.n. 08193 Cerdanyola del Vallés Barcelona Spain
  • Jean‐Didier Maréchal
    Departament de Química Universitat Autònoma de Barcelona Edifici C.n. 08193 Cerdanyola del Vallés Barcelona Spain
  • Andy‐Mark W. H. Thunnissen
    Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands
  • Gerard Roelfes
    Stratingh Institute for Chemistry University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands

書誌事項

公開日
2018-05-29
権利情報
  • http://creativecommons.org/licenses/by-nc/4.0/
DOI
  • 10.1002/anie.201802946
公開者
Wiley

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説明

<jats:title>Abstract</jats:title><jats:p>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.</jats:p>

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