Catalytic and structural features of flavoprotein hydroxylases and epoxidases

S. Montersino, D. Tischler, G.T. Gassner, W.J.H. van Berkel

Research output: Contribution to journalArticleAcademicpeer-review

78 Citations (Scopus)

Abstract

Monooxygenases perform chemo-, regio- and/or enantioselective oxygenations of organic substrates under mild reaction conditions. These properties and the increasing number of representatives along with effective preparation methods place monooxygenases in the focus of industrial biocatalysis. Mechanistic and structural insights reveal reaction sequences and allow turning them into efficient tools for the production of valuable products. Herein we describe two biocatalytically relevant subclasses of flavoprotein monooxygenases with a close evolutionary relation: subclass A represented by p-hydroxybenzoate hydroxylase (PHBH) and subclass E formed by styrene monooxygenases (SMOs). PHBH family members perform highly regioselective hydroxylations on a wide variety of aromatic compounds. The more recently discovered SMOs catalyze a number of stereoselective epoxidation and sulfoxidation reactions. Mechanistic and structural studies expose distinct characteristics, which provide a promising source for future biocatalyst development.
Original languageEnglish
Pages (from-to)2301-2319
JournalAdvanced Synthesis and Catalysis
Volume353
Issue number13
DOIs
Publication statusPublished - 2011

Keywords

  • p-hydroxybenzoate hydroxylase
  • 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
  • recombinant escherichia-coli
  • fad-dependent monooxygenase
  • rhodococcus-opacus 1cp
  • whole-cell biocatalyst
  • styrene monooxygenase
  • phenol hydroxylase
  • crystal-structure

Fingerprint

Dive into the research topics of 'Catalytic and structural features of flavoprotein hydroxylases and epoxidases'. Together they form a unique fingerprint.

Cite this