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Citation
Tags
HERO ID
5068525
Reference Type
Journal Article
Subtype
Letter
Title
Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
Author(s)
Pesic, M; Willot, SJ; Fernández-Fueyo, E; Tieves, F; Alcalde, M; Hollmann, F
Year
2019
Is Peer Reviewed?
Yes
Journal
Zeitschrift fuer Naturforschung C
ISSN:
0939-5075
Volume
74
Issue
3-4
Page Numbers
101-104
Language
English
PMID
30379645
DOI
10.1515/znc-2018-0137
Web of Science Id
WOS:000459670900007
Abstract
There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we report a multienzymatic cascade for in situ generation of hydrogen peroxide. In the first step, in the presence of NAD+ cofactor, formate dehydrogenase from Candida boidinii (FDH) catalysed the oxidation of formate yielding CO2. Reduced NADH was reoxidised by the reduction of the flavin mononucleotide cofactor bound to an old yellow enzyme homologue from Bacillus subtilis (YqjM), which subsequently reacts with molecular oxygen yielding hydrogen peroxide. Finally, this system was coupled to the hydroxylation of ethylbenzene reaction catalysed by an evolved peroxygenase from Agrocybe aegerita (rAaeUPO). Additionally, we studied the influence of different reaction parameters on the performance of the cascade with the aim of improving the turnover of the hydroxylation reaction.
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Ethylbenzene
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