Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

J Biotechnol. 2006 Aug 5;124(4):670-89. doi: 10.1016/j.jbiotec.2006.03.044. Epub 2006 May 19.


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.

Publication types

  • Review

MeSH terms

  • Catalysis
  • Electron-Transferring Flavoproteins / chemistry*
  • Mixed Function Oxygenases / chemistry*
  • Structure-Activity Relationship
  • Substrate Specificity


  • Electron-Transferring Flavoproteins
  • Mixed Function Oxygenases