A one-electron oxidation of carcinogenic nonaminoazo dye Sudan I by horseradish peroxidase
Language English Country Sweden Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18987613
PII: NEL290508A07
Knihovny.cz E-resources
- MeSH
- Chromatography, Thin Layer MeSH
- Electrons MeSH
- Spectrometry, Mass, Electrospray Ionization MeSH
- Mass Spectrometry MeSH
- Carcinogens chemistry MeSH
- Horseradish Peroxidase chemistry MeSH
- Magnetic Resonance Spectroscopy MeSH
- Naphthols chemistry MeSH
- Oxidation-Reduction MeSH
- Hydrogen Peroxide chemistry MeSH
- Spectrophotometry, Ultraviolet MeSH
- Chromatography, High Pressure Liquid MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 1-phenylazo-2-naphthol MeSH Browser
- Carcinogens MeSH
- Horseradish Peroxidase MeSH
- Naphthols MeSH
- Hydrogen Peroxide MeSH
OBJECTIVES: The aim of the study was to examine oxidation of carcinogenic Sudan I by peroxidase and characterize the structure of its two major peroxidasemediated metabolites. Another target of the study was to evaluate a mechanism of this oxidation. METHODS: Thin layer chromatography (TLC) and high performance liquid chromatography (HPLC) with ultraviolet (UV) and visible (VIS) detection was employed for the separation of Sudan I metabolites formed by peroxidase. UV/ VIS-, and mass- spectroscopy as well as nuclear magnetic resonance (NMR) were used to characterize structures of two major Sudan I metabolites. RESULTS: Peroxidase oxidizes Sudan I by a one electron oxidation to eight products. Two major Sudan I metabolites were isolated by TLC on silica gel and HPLC and structurally characterized. The major product formed during the Sudan I oxidation by peroxidase is Sudan I metabolite M2, which corresponds to a Sudan I dimer molecule. The second major metabolite (M1) is the product of secondary, enzyme independent reactions, being formed from the Sudan I dimer that lost the benzenediazonium moiety. CONCLUSIONS: The data are the first report on structural characterization of Sudan I metabolites formed by its oxidation with peroxidase.
