Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/136085
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Type: | Journal article |
Title: | Selective oxidations using a cytochrome P450 enzyme variant driven with surrogate oxygen donors and light |
Author: | Lee, J. Podgorski, M. Moir, M. Gee, A.R. Bell, S.G. |
Citation: | Chemistry: A European Journal, 2022; 28(49):1-9 |
Publisher: | Wiley |
Issue Date: | 2022 |
ISSN: | 0947-6539 1521-3765 |
Statement of Responsibility: | Joel H. Z. Lee, Matthew N. Podgorski, Michae lMoir, Alecia R. Gee, and Stephen G. Bell |
Abstract: | Cytochrome P450 monooxygenase enzymes are versatile catalysts, which have been adapted for multiple applications in chemical synthesis. Mutation of a highly conserved active site threonine to a glutamate can convert these enzymes into peroxygenases that utilise hydrogen peroxide (H2O2). Here, we use the T252E-CYP199A4 variant to study peroxide-driven oxidation activity by using H2O2 and urea-hydrogen peroxide (UHP). We demonstrate that the T252E variant has a higher stability to H2O2 in the presence of substrate that can undergo carbon-hydrogen abstraction. This peroxygenase variant could efficiently catalyse O-demethylation and an enantioselective epoxidation reaction (94 % ee). Neither the monooxygenase nor peroxygenase pathways of the P450 demonstrated a significant kinetic isotope effect (KIE) for the oxidation of deuterated substrates. These new peroxygenase variants offer the possibility of simpler cytochrome P450 systems for selective oxidations. To demonstrate this, a light driven H2O2 generating system was used to support efficient product formation with this peroxygenase enzyme. |
Keywords: | biocatalysis; hemeenzymes; monooxygenases; peroxygenases; protein engineering |
Description: | Version of record online: July 14, 2022 |
Rights: | © 2022 The Authors.Chemistry- A European Journal published by Wiley-VCHGmbH This is an open access article under the terms of the Creative Commons Attribution Non-Commercial License,which permits use, distribution and reproduction in any medium,provided the original work is properly cited and is not used for commercial purposes. |
DOI: | 10.1002/chem.202201366 |
Grant ID: | http://purl.org/au-research/grants/arc/DP200102411 |
Published version: | http://dx.doi.org/10.1002/chem.202201366 |
Appears in Collections: | Chemistry publications |
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hdl_136085.pdf | Published version | 2.37 MB | Adobe PDF | View/Open |
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