Structural highlights
Publication Abstract from PubMed
An artificial heme enzyme was created by 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. Yet, good catalytic activity and moderate enantioselectivity was observed in the abiological cyclopropanation reaction. We proposed 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 allowing for binding of substrates and formation of pre-catalytic structures.
An Artificial Heme Enzyme for Cyclopropanation Reactions.,Villarino L, Splan K, Reddem E, Gutierrez de Souza C, Alonso-Cotchico L, Lledos A, Marechal JD, Thunnissen AM, Roelfes G Angew Chem Int Ed Engl. 2018 May 2. doi: 10.1002/anie.201802946. PMID:29719099[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Villarino L, Splan K, Reddem E, Gutierrez de Souza C, Alonso-Cotchico L, Lledos A, Marechal JD, Thunnissen AM, Roelfes G. An Artificial Heme Enzyme for Cyclopropanation Reactions. Angew Chem Int Ed Engl. 2018 May 2. doi: 10.1002/anie.201802946. PMID:29719099 doi:http://dx.doi.org/10.1002/anie.201802946
