An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata
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چکیده
منابع مشابه
Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata
The marine globin dehaloperoxidase-hemoglobin (DHP) from Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of monohaloindoles, a previously unknown class of substrate for DHP. Using 5-Br-indole as a representative substrate, the major monooxygenated products were found to be 5-Br-2-oxindole and 5-Br-3-oxindolenine. Isotope labeling studies confirmed that the oxygen atom incor...
متن کاملEnzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding.
Amphitrite ornata dehaloperoxidase (DHP) is a heme enzyme with a globin structure, which is capable of oxidizing para-halogenated phenols to the corresponding quinones. Cloning, high-level expression, and purification of recombinant DHP are described. Recombinant DHP was assayed by stopped-flow experiments for its ability to oxidatively debrominate 2,4,6-tribromophenol (TBP). The enzymatic acti...
متن کاملThe pH dependence of the activity of dehaloperoxidase from Amphitrite ornata.
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 ...
متن کاملSubstrate binding triggers a switch in the iron coordination in dehaloperoxidase from Amphitrite ornata: HYSCORE experiments.
We have explored the effect of substrate binding on the heme iron conformation in the enzyme dehaloperoxidase (DHP) that was first isolated from the terebellid polychaete Amphitrite ornata and is now expressed in Escherichia coli.1-3 DHP is a dimeric hemoglobin4 that also has significant peroxidase activity under physiological conditions.5 Since hemoglobins and peroxidases require ferrous and f...
متن کاملSpectroscopic study of substrate binding to the carbonmonoxy form of dehaloperoxidase from Amphitrite ornata.
Dehaloperoxidase (DHP) is a globular heme enzyme found in the marine worm Amphitrite ornata that can catalyze the dehalogenation of halophenols to the corresponding quinones by using hydrogen peroxide as a cosubstrate. Its three-dimensional fold is surprisingly similar to that of the oxygen storage protein myoglobin (Mb). A key structural feature common to both DHP and Mb is the existence of mu...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.9.4609