An Artificial Heme Enzyme for Cyclopropanation Reactions
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...
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Published in | Angewandte Chemie International Edition Vol. 57; no. 26; pp. 7785 - 7789 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Germany
Wiley Subscription Services, Inc
25.06.2018
John Wiley and Sons Inc |
Edition | International ed. in English |
Subjects | |
Online Access | Get full text |
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Summary: | 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.
Get a move on: An artificial heme enzyme based on the lactococcal multidrug resistance regulator (LmrR; blue/green) was created through self‐assembly and shows good activity in cyclopropanation reactions. The dynamics of the system are of key importance for its activity. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201802946 |