Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions

[EN] 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,...

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Autores: Pesic, Milja, Willot, S.J.P., Fernández-Fueyo, Elena, Tieves, Florian, Alcalde Galeote, Miguel, Hollmann, Frank
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/214986
Acceso en línea:http://hdl.handle.net/10261/214986
Access Level:acceso abierto
Palabra clave:Formate dehydrogenase
Hydrogen peroxide generation
Old yellow enzyme
Oxyfunctionalisation
Peroxygenase.
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spelling Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactionsPesic, MiljaWillot, S.J.P.Fernández-Fueyo, ElenaTieves, FlorianAlcalde Galeote, MiguelHollmann, FrankFormate dehydrogenaseHydrogen peroxide generationOld yellow enzymeOxyfunctionalisationPeroxygenase.[EN] 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.Financial support by the European Research Council (ERC Consolidator Grant No. 648026) is gratefully acknowledged.Walter de GruyterEuropean Research CouncilAlcalde Galeote, Miguel [0000-0001-6780-7616]Hollmann, Frank [0000-0003-4821-756X]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020192020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/214986reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/EC/H2020/648026http://dx.doi.org/10.1515/znc-2018-0137Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2149862026-05-22T06:33:51Z
dc.title.none.fl_str_mv Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
title Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
spellingShingle Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
Pesic, Milja
Formate dehydrogenase
Hydrogen peroxide generation
Old yellow enzyme
Oxyfunctionalisation
Peroxygenase.
title_short Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
title_full Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
title_fullStr Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
title_full_unstemmed Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
title_sort Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions
dc.creator.none.fl_str_mv Pesic, Milja
Willot, S.J.P.
Fernández-Fueyo, Elena
Tieves, Florian
Alcalde Galeote, Miguel
Hollmann, Frank
author Pesic, Milja
author_facet Pesic, Milja
Willot, S.J.P.
Fernández-Fueyo, Elena
Tieves, Florian
Alcalde Galeote, Miguel
Hollmann, Frank
author_role author
author2 Willot, S.J.P.
Fernández-Fueyo, Elena
Tieves, Florian
Alcalde Galeote, Miguel
Hollmann, Frank
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv European Research Council
Alcalde Galeote, Miguel [0000-0001-6780-7616]
Hollmann, Frank [0000-0003-4821-756X]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Formate dehydrogenase
Hydrogen peroxide generation
Old yellow enzyme
Oxyfunctionalisation
Peroxygenase.
topic Formate dehydrogenase
Hydrogen peroxide generation
Old yellow enzyme
Oxyfunctionalisation
Peroxygenase.
description [EN] 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/214986
url http://hdl.handle.net/10261/214986
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/EC/H2020/648026
http://dx.doi.org/10.1515/znc-2018-0137
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Walter de Gruyter
publisher.none.fl_str_mv Walter de Gruyter
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.198674

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