Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications

D.E. Torres Pazmino, M. Winkler, A. Glieder, M. W. Fraaije*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

163 Citations (Scopus)
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Abstract

Monooxygenases are enzymes that catalyze the insertion of a single oxygen atom from O(2) into an organic substrate. In order to carry out this type of reaction, these enzymes need to activate molecular oxygen to overcome its spin-forbidden reaction with the organic substrate. In most cases, monooxygenases utilize (in)organic cofactors to transfer electrons to molecular oxygen for its activation. Monooxygenases typically are highly chemo-, regio-, and/or enantioselective, making them attractive biocatalysts. In this review, an exclusive overview of known monooxygenases is presented, based on the type of cofactor that these enzymes require. This includes not only the cytochrome P450 and Flavin-dependent monooxygenases, but also enzymes that utilize pterin, metal ions (copper or iron) or no cofactor at all. As most of these monooxygenases require nicotinamide coenzymes as electron donors, also an overview of current methods for coenzyme regeneration is given. This latter overview is of relevance for the biotechnological applications of these oxidative enzymes. (C) 2010 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)9-24
Number of pages16
JournalJournal of Biotechnology
Volume146
Issue number1-2
DOIs
Publication statusPublished - Mar-2010

Keywords

  • Biocatalysis
  • Coenzyme regeneration
  • Cofactors
  • Copper-dependent monooxygenases
  • Flavin-dependent monooxygenases
  • Non-heme iron-dependent monooxygenases
  • P450 monooxygenases
  • Pterin monooxygenases
  • ALPHA-HYDROXYLATING MONOOXYGENASE
  • PARTICULATE METHANE MONOOXYGENASE
  • BAEYER-VILLIGER MONOOXYGENASES
  • RECOMBINANT ESCHERICHIA-COLI
  • NADPH-ADRENODOXIN REDUCTASE
  • DOPAMINE-BETA-HYDROXYLASE
  • ADENOSYL-L-METHIONINE
  • PHOSPHITE DEHYDROGENASE
  • CRYSTAL-STRUCTURE
  • PSEUDOMONAS-OLEOVORANS

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