FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase

D. Tischler, M. Schlömann, W.J.H. van Berkel, G.T. Gassner

Research output: Contribution to journalArticleAcademicpeer-review

13 Citations (Scopus)

Abstract

StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.
Original languageEnglish
Pages (from-to)3848-3852
JournalFEBS Letters
Volume587
Issue number23
DOIs
Publication statusPublished - 2013

Keywords

  • rhodococcus-opacus 1cp
  • phenol hydroxylase
  • wild-type
  • mechanism

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