Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding
| Autor: | Jennifer Belyea, Michael F. Davis, Lauren B. Gilvey, Marisha L. Godek, Stefan Franzen, Steven A. Lommel, Tim L. Sit |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
endocrine system
Biochemistry Horseradish peroxidase Cofactor Hemoglobins chemistry.chemical_compound Phenols Escherichia coli Animals Globin Cloning Molecular Heme biology Substrate (chemistry) Polychaeta Hydrogen Peroxide Amphitrite ornata biology.organism_classification Recombinant Proteins Globins Enzyme Activation Peroxidases chemistry Myoglobin biology.protein Protein Binding Peroxidase |
| Zdroj: | Biochemistry. 44:15637-15644 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | 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 activity of the ferric form of recombinant DHP is intermediate between that of a typical peroxidase (horseradish peroxidase) and a typical globin (horse heart myoglobin). The present study shows that, unlike other known peroxidases, DHP activity requires the addition of substrate, TBP, prior to the cosubstrate, peroxide. The presence of a substrate-binding site in DHP is consistent with a two-electron oxidation mechanism and an obligatory order for activation of the enzyme by addition of the substrate prior to the cosubstrate. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|