Baeyer-Villiger Monooxygenases: Tunable Oxidative Biocatalysts

Maximilian J. L. J. Furst, Alejandro Gran-Scheuch, Friso S. Aalbers, Marco W. Fraaije*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

18 Citations (Scopus)
168 Downloads (Pure)

Abstract

Pollution, accidents, and misinformation have earned the pharmaceutical and chemical industry a poor public reputation, despite their undisputable importance to society. Biotechnological advances hold the promise to enable a future of drastically reduced environmental impact and rigorously more efficient production routes at the same time. This is exemplified in the Baeyer-Villiger reaction, which offers a simple synthetic route to oxidize ketones to esters, but application is hampered by the requirement of hazardous and dangerous reagents. As an attractive alternative, flavin-containing Baeyer-Villiger monooxygenases (BVMOs) have been investigated for their potential as biocatalysts for a long time, and many variants have been characterized. After a general look at the state of biotechnology, we here summarize the literature on biochemical characterizations, mechanistic and structural investigations, as well as enzyme engineering efforts in BVMOs. With a focus on recent developments, we critically outline the advances toward tuning these enzymes suitable for industrial applications.

Original languageEnglish
Pages (from-to)11207-11241
Number of pages69
JournalACS Catalysis
Volume9
Issue number12
DOIs
Publication statusPublished - Dec-2019

Keywords

  • Baeyer-Villiger
  • ketone oxidation
  • peroxyflavin
  • cyclohexanone monooxygenase
  • phenylacetone monooxygenase
  • biocatalysis
  • protein engineering
  • FLAVIN-CONTAINING MONOOXYGENASES
  • PSEUDOMONAS-FLUORESCENS ACB
  • RADICICOLA ATCC 11011
  • CYCLOHEXANONE MONOOXYGENASE
  • PHENYLACETONE-MONOOXYGENASE
  • DIRECTED EVOLUTION
  • EPSILON-CAPROLACTONE
  • CRYSTAL-STRUCTURE
  • STEROID MONOOXYGENASE
  • FLAVOPROTEIN MONOOXYGENASES

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