Efficient biocatalytic C-H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450

Simple item page
dc.contributor.authorGee, A.R.
dc.contributor.authorStone, I.
dc.contributor.authorStockdale, T.P.
dc.contributor.authorPukala, T.L.
dc.contributor.authorDe Voss, J.J.
dc.contributor.authorBell, S.G.
dc.date.issued2023
dc.description.abstractA highly sought after reaction in chemical synthesis is the activation of unactivated carbon–hydrogen bonds. We demonstrate the hydroxylation of fatty acids using an engineered thermostable archaeal cytochrome P450 enzyme. By replacing a seven amino acid section of the I-helix, the nicotinamide cofactor-dependent monooxygenase was converted into a hydrogen peroxide using peroxygenase, enabling the efficient biocatalytic oxidation of C–H bonds at room temperature to 90 °C.
dc.description.statementofresponsibilityAlecia R. Gee, Isobella S. J. Stone, Tegan P. Stockdale, Tara L. Pukala, James J. De Voss and Stephen G. Bell
dc.identifier.citationChemical Communications, 2023; 59(90):13486-13489
dc.identifier.doi10.1039/d3cc04626e
dc.identifier.issn1359-7345
dc.identifier.issn1364-548X
dc.identifier.orcidGee, A.R. [0000-0001-8034-2817]
dc.identifier.orcidStone, I. [0000-0002-9474-4961]
dc.identifier.orcidPukala, T.L. [0000-0001-7391-1436]
dc.identifier.orcidBell, S.G. [0000-0002-7457-9727]
dc.identifier.urihttps://hdl.handle.net/2440/139892
dc.language.isoen
dc.publisherRoyal Society of Chemistry
dc.relation.granthttp://purl.org/au-research/grants/arc/DP200102411
dc.rightsThis journal is © The Royal Society of Chemistry 2023
dc.source.urihttps://doi.org/10.1039/d3cc04626e
dc.subjectHeme
dc.subjectCytochrome P-450 Enzyme System
dc.subjectOxidation-Reduction
dc.subjectHydroxylation
dc.subjectBiocatalysis
dc.titleEfficient biocatalytic C-H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450
dc.typeJournal article
pubs.publication-statusPublished

Files

Collections

Chemistry publications