Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

W.J.H. van Berkel, N.M. Kamerbeek, M.W. Fraaije

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475 Citations (Scopus)


During the last decades a large number of flavin-dependent monooxygenases have been isolated and studied. This has revealed that flavoprotein monooxygenases are able to catalyze a remarkable wide variety of oxidative reactions such as regioselective hydroxylations and enantioselective sulfoxidations. These oxidation reactions are often difficult, if not impossible, to be achieved using chemical approaches. Analysis of the available genome sequences has indicated that many more flavoprotein monooxygenases exist and await biocatalytic exploration. Based on the known biochemical properties of a number of flavoprotein monooxygenases and sequence and structural analyses, flavoprotein monooxygenases can be classified into six distinct flavoprotein monooxygenase subclasses. This review provides an inventory of known flavoprotein monooxygenases belonging to these different enzyme subclasses. Furthermore, the biocatalytic potential of a selected number of flavoprotein monooxygenases is highlighted
Original languageEnglish
Pages (from-to)670-689
JournalJournal of Biotechnology
Issue number4
Publication statusPublished - 2006


  • baeyer-villiger monooxygenases
  • flavin-containing monooxygenase
  • vanillyl-alcohol oxidase
  • para-hydroxybenzoate hydroxylase
  • encoding nitrilotriacetate monooxygenase
  • p-hydroxyphenylacetate 3-hydroxylase
  • bacillus-thermoglucosidasius a7
  • tryptophan 7-halo

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