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Issue 5, 2011
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Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase

Ana Rioz-Martínez,a  Malgorzata Kopacz,b  Gonzalo de Gonzalo,*b  Daniel E. Torres Pazmiño,b  Vicente Gotora  and  Marco W. Fraaije*b 
Author affiliations

* Corresponding authors

a Departamento de Química Orgánica e Inorgánica, Instituto Universitario de Biotecnología de Asturias, Universidad de Oviedo, C/Julián Clavería 8, Oviedo, Spain

b Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen, The Netherlands
E-mail: g.de.gonzalo.calvo@rug.nl, m.w.fraaije@rug.nl
Fax: +31 50 363 4165
Tel: +31 50 363 4345

Abstract

A bacterial flavin-containing monooxygenase (FMO), fused to phosphite dehydrogenase, has been used to explore its biocatalytic potential. The bifunctional biocatalyst could be expressed in high amounts in Escherichia coli and was able to oxidize indole and indole derivatives into a variety of indigo compounds. The monooxygenase also performs the sulfoxidation of a wide range of prochiral sulfides, showing moderate to good enantioselectivities in forming chiral sulfoxides.

Graphical abstract: Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase

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Publication details

The article was received on 05 Nov 2010, accepted on 15 Dec 2010 and first published on 11 Jan 2011


Article type: Communication
DOI: 10.1039/C0OB00988A
Citation: Org. Biomol. Chem., 2011,9, 1337-1341
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    Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase

    A. Rioz-Martínez, M. Kopacz, G. de Gonzalo, D. E. Torres Pazmiño, V. Gotor and M. W. Fraaije, Org. Biomol. Chem., 2011, 9, 1337
    DOI: 10.1039/C0OB00988A

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