Nonmicrobial Nitrophenol Degradation via Peroxygenase Activity of Dehaloperoxidase-Hemoglobin from Amphitrite ornata
| Autor: | Leiah M. Carey, Reza A. Ghiladi, Nikolette L. McCombs, Jennifer D'Antonio, David A. Barrios |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Stereochemistry 010402 general chemistry 01 natural sciences Biochemistry Catalysis Cofactor Mixed Function Oxygenases Nitrophenols Hemoglobins 03 medical and health sciences Nitrophenol chemistry.chemical_compound medicine Animals Heme 030102 biochemistry & molecular biology biology Substrate (chemistry) Polychaeta Hydrogen Peroxide Amphitrite ornata biology.organism_classification 0104 chemical sciences Oxygen Peroxidases chemistry biology.protein Ferric Oxidation-Reduction Peroxidase medicine.drug |
| Zdroj: | Biochemistry. 55:2465-2478 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | The marine hemoglobin dehaloperoxidase (DHP) from Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of nitrophenols, an unprecedented nonmicrobial degradation pathway for nitrophenols by a hemoglobin. Using 4-nitrophenol (4-NP) as a representative substrate, the major monooxygenated product was 4-nitrocatechol (4-NC). Isotope labeling studies confirmed that the O atom incorporated was derived exclusively from H2O2, indicative of a peroxygenase mechanism for 4-NP oxidation. Accordingly, X-ray crystal structures of 4-NP (1.87 Å) and 4-NC (1.98 Å) bound to DHP revealed a binding site in close proximity to the heme cofactor. Peroxygenase activity could be initiated from either the ferric or oxyferrous states with equivalent substrate conversion and product distribution. The 4-NC product was itself a peroxidase substrate for DHP, leading to the secondary products 5-nitrobenzene-triol and hydroxy-5-nitro-1,2-benzoquinone. DHP was able to react with 2,4-dinitrophenol (2,4-DNP) but was unreactive against 2,4,6-trinitrophenol (2,4,6-TNP). pH dependence studies demonstrated increased reactivity at lower pH for both 4-NP and 2,4-DNP, suggestive of a pH effect that precludes the reaction with 2,4,6-TNP at or near physiological conditions. Stopped-flow UV-visible spectroscopic studies strongly implicate a role for Compound I in the mechanism of 4-NP oxidation. The results demonstrate that there may be a much larger number of nonmicrobial enzymes that are underrepresented when it comes to understanding the degradation of persistent organic pollutants such as nitrophenols in the environment. |
| Databáze: | OpenAIRE |
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