The pH dependence of the activity of dehaloperoxidase from Amphitrite ornata.

@article{Franzen2007ThePD,
  title={The pH dependence of the activity of dehaloperoxidase from Amphitrite ornata.},
  author={Stefan Franzen and Lauren B G Gilvey and Jennifer L Belyea},
  journal={Biochimica et biophysica acta},
  year={2007},
  volume={1774 1},
  pages={121-30}
}
Dehaloperoxidase (DHP) from the terebellid polychaete, Amphitrite ornata, is the first hemoglobin that has peroxidase activity as part of its native function. The substrate 2,4,6-tribromophenol (TBP) is oxidatively debrominated by DHP to form 2,6-dibromoquinone (DBQ) in a two-electron process. There is a well-defined internal binding site for TBP above the heme, a feature not observed in other hemoglobins or peroxidases. A study of the pH dependence of the activity of DHP reveals a substantial… CONTINUE READING

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