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Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications

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dc.citation.titleFrontiers in Microbiology
dc.citation.volume1-14
dc.citation.volume5
dc.creatorCeccoli, Romina Denis
dc.creatorBianchi, Dario A.
dc.creatorRial, Daniela V.
dc.date.accessioned2024-04-16T15:45:59Z
dc.date.available2024-04-16T15:45:59Z
dc.date.issued2014-02-06
dc.description.abstractExternal flavoprotein monooxygenases comprise a group of flavin-dependent oxidoreductases that catalyze the insertion of one atom of molecular oxygen into an organic substrate and the second atom is reduced to water. These enzymes are involved in a great number of metabolic pathways both in prokaryotes and eukaryotes. Flavoprotein monooxygenases have attracted the attention of researchers for several decades and the advent of recombinant DNA technology caused a great progress in the field. These enzymes are subjected to detailed biochemical and structural characterization and some of them are also regarded as appealing oxidative biocatalysts for the production of fine chemicals and valuable intermediates toward active pharmaceutical ingredients due to their high chemo-, stereo-, and regioselectivity. Here, we review the most representative reactions catalyzed both in vivo and in vitro by prototype flavoprotein monooxygenases, highlighting the strategies employed to produce them recombinantly, to enhance the yield of soluble proteins, and to improve cofactor regeneration in order to obtain versatile biocatalysts. Although we describe the most outstanding features of flavoprotein monooxygenases, we mainly focus on enzymes that were cloned, expressed and used for biocatalysis during the last years.
dc.description.filFil: Ceccoli, Romina Denis. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Ciencias Biológicas. Área Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina.
dc.description.filFil: Bianchi, Dario A. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Orgánica. Área Análisis de Medicamentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química Rosario (CONICET-IQUIR); Argentina.
dc.description.filFil: Rial, Daniela V. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Ciencias Biológicas. Área Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PRH 24 PICT 2009-0088
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET): PIP 2012-2014 1156
dc.description.sponsorshipUniversidad Nacional de Rosario (UNR): BIO287, BIO339
dc.identifier.issn1664-302X
dc.identifier.urihttps://hdl.handle.net/2133/26894
dc.language.isoen
dc.publisherFrontiers Media
dc.relation.publisherversionhttps://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2014.00025/full
dc.relation.publisherversionhttps://doi.org/10.3389/fmicb.2014.00025
dc.rightsopenAccess
dc.rights.holderCeccoli, Romina Denis
dc.rights.holderBianchi, Dario A.
dc.rights.holderRial, Daniela V.
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectFlavoprotein monooxygenase
dc.subjectBaeyer–Villiger oxidation
dc.subjectBiooxidations
dc.subjectBiocatalysis
dc.subjectSulfoxidation
dc.subjectEpoxidation
dc.subjectHydroxylation
dc.subjectRecombinant biocatalyst
dc.titleFlavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications
dc.typearticulo
dc.type.collectionarticulo
dc.type.versionpublishedVersion

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