Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/120169
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Type: Journal article
Title: The effect of decoy molecules on the activity of the P450Bm3 holoenzyme and a heme domain peroxygenase variant
Author: Dezvarei, S.
Shoji, O.
Watanabe, Y.
Bell, S.
Citation: Catalysis Communications, 2019; 124:97-102
Publisher: Elsevier
Issue Date: 2019
ISSN: 1566-7367
1873-3905
Statement of
Responsibility: 
Shaghayegh Dezvarei, Osami Shoji, Yoshihito Watanabe, Stephen G.Bell
Abstract: Perfluorinated 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.
Keywords: Cytochrome P450 monooxygenase; hydroxylation; peroxygenase; epoxidation; sulfoxidation; biocatalysis
Rights: © 2019 Elsevier B.V. All rights reserved.
RMID: 0030111689
DOI: 10.1016/j.catcom.2019.03.004
Grant ID: http://purl.org/au-research/grants/arc/FT140100355
Appears in Collections:Chemical Engineering publications

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