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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q2IU02_RHOP2 Q2IU02_RHOP2] | | [https://www.uniprot.org/uniprot/Q2IU02_RHOP2 Q2IU02_RHOP2] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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 (H(2) O(2) ). Here, we use the T252E-CYP199A4 variant to study peroxide-driven oxidation activity by using H(2) O(2) and urea-hydrogen peroxide (UHP). We demonstrate that the T252E variant has a higher stability to H(2) O(2) 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 H(2) O(2) generating system was used to support efficient product formation with this peroxygenase enzyme.
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| Selective Oxidations Using a Cytochrome P450 Enzyme Variant Driven with Surrogate Oxygen Donors and Light.,Lee JHZ, Podgorski MN, Moir M, Gee AR, Bell SG Chemistry. 2022 Sep 1;28(49):e202201366. doi: 10.1002/chem.202201366. Epub 2022 , Jul 14. PMID:35712785<ref>PMID:35712785</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8d1c" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
