An Artificial Heme Enzyme for Cyclopropanation Reactions
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.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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An Artificial Heme Enzyme for Cyclopropanation Reactions ; volume:130 ; number:26 ; year:2018 ; pages:7911-7915 ; extent:5
Angewandte Chemie ; 130, Heft 26 (2018), 7911-7915 (gesamt 5)
- Urheber
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Villarino, Lara
Splan, Kathryn E.
Reddem, Eswar
Alonso‐Cotchico, Lur
Gutiérrez de Souza, Cora
Lledós, Agustí
Maréchal, Jean‐Didier
Thunnissen, Andy‐Mark W. H.
Roelfes, Gerard
- DOI
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10.1002/ange.201802946
- URN
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urn:nbn:de:101:1-2022090806444770193693
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2005, 07:38 MESZ
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Beteiligte
- Villarino, Lara
- Splan, Kathryn E.
- Reddem, Eswar
- Alonso‐Cotchico, Lur
- Gutiérrez de Souza, Cora
- Lledós, Agustí
- Maréchal, Jean‐Didier
- Thunnissen, Andy‐Mark W. H.
- Roelfes, Gerard
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Unexpected photosensitivity of the well-characterized heme enzyme chlorite dismutase
Energy relationships in enzyme reactions
Can enzyme proximity accelerate cascade reactions?
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