4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds.

@article{Kamerbeek20014HydroxyacetophenoneMF,
  title={4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds.},
  author={Nanne M. Kamerbeek and Mari{\"e}lle J H Moonen and J G van der Ven and Willem J H van Berkel and Marco W Fraaije and Dick B. Janssen},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 9},
  pages={2547-57}
}
A novel flavoprotein that catalyses the NADPH-dependent oxidation of 4-hydroxyacetophenone to 4-hydroxyphenyl acetate, was purified to homogeneity from Pseudomonas fluorescens ACB. Characterization of the purified enzyme showed that 4-hydroxyacetophenone monooxygenase (HAPMO) is a homodimer of approximately 140 kDa with each subunit containing a noncovalently bound FAD molecule. HAPMO displays a tight coupling between NADPH oxidation and substrate oxygenation. Besides 4-hydroxyacetophenone a… CONTINUE READING