Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/120169
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dc.contributor.authorDezvarei, S.-
dc.contributor.authorShoji, O.-
dc.contributor.authorWatanabe, Y.-
dc.contributor.authorBell, S.G.-
dc.date.issued2019-
dc.identifier.citationCatalysis Communications, 2019; 124:97-102-
dc.identifier.issn1566-7367-
dc.identifier.issn1873-3905-
dc.identifier.urihttp://hdl.handle.net/2440/120169-
dc.description.abstractPerfluorinated decoy molecules based on a combination of fatty and amino acids were used to enhance hydroxylation, epoxidation and sulfoxidation reactions of P450Bm3. The combination of amino acid derived second generation decoy molecules, with the rate accelerating variant R19 (R47L/Y51F/H171L/Q307H/N319Y) displayed the highest oxidation rates. Mutation of Thr268 to Glu (Bm3TE) converted the heme domain to a H₂O₂ utilising peroxygenase. This Bm3TE variant displayed significant peroxygenase activity towards all the substrates tested with a preference for methylthiobenzene sulfoxidation. However, the addition of decoy molecules did not improve the efficiency of this variant.-
dc.description.statementofresponsibilityShaghayegh Dezvarei, Osami Shoji, Yoshihito Watanabe, Stephen G.Bell-
dc.language.isoen-
dc.publisherElsevier-
dc.rights© 2019 Elsevier B.V. All rights reserved.-
dc.source.urihttp://dx.doi.org/10.1016/j.catcom.2019.03.004-
dc.subjectCytochrome P450 monooxygenase; hydroxylation; peroxygenase; epoxidation; sulfoxidation; biocatalysis-
dc.titleThe effect of decoy molecules on the activity of the P450Bm3 holoenzyme and a heme domain peroxygenase variant-
dc.typeJournal article-
dc.identifier.doi10.1016/j.catcom.2019.03.004-
dc.relation.granthttp://purl.org/au-research/grants/arc/FT140100355-
pubs.publication-statusPublished-
dc.identifier.orcidDezvarei, S. [0000-0002-9634-075X]-
dc.identifier.orcidBell, S.G. [0000-0002-7457-9727]-
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Chemical Engineering publications

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