Catalytic and hydrodynamic properties of styrene monooxygenases from Rhocodoccus opacus 1CP are modulated by cofactor binding.

A. Riedel, T. Heine, A.H. Westphal, C. Conrad, P. Rathsack, W.J.H. van Berkel, D. Tischler

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)

Abstract

Styrene monooxygenases (SMOs) are flavoenzymes catalyzing the epoxidation of styrene into styrene oxide. SMOs are composed of a monooxygenase (StyA) and a reductase (StyB). The latter delivers reduced FAD to StyA on the expense of NADH. We identified Rhodococcus opacus 1CP as the first microorganism to possess three different StyA isoforms occurring in two systems StyA1/StyA2B and StyA/StyB, respectively. The hydrodynamic properties of StyA isozymes were found to be modulated by the binding of the (reduced) FAD cofactor. StyA1 and SyA2B mainly occur as dimers in their active forms while StyA is a monomer. StyA1 showed the highest epoxidation activity and excellent enantioselectivity in aromatic sulfoxidation. The hydrodynamic and biocatalytic properties of SMOs from strain 1CP are of relevance for investigation of possible industrial applications.
Original languageEnglish
Article number30
Number of pages11
JournalAMB Express
Volume5
DOIs
Publication statusPublished - 2015

Keywords

  • recombinant escherichia-coli
  • pseudomonas-fluorescens st
  • functional-analysis
  • crystal-structure
  • catabolism genes
  • strain vlb120
  • putida ca-3
  • degradation
  • mechanism
  • oxide

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