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|Title:||The effect of decoy molecules on the activity of the P450Bm3 holoenzyme and a heme domain peroxygenase variant|
|Citation:||Catalysis Communications, 2019; 124:97-102|
|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.|
|Appears in Collections:||Chemical Engineering publications|
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