Resumen
In the presence of hydrogen peroxide (H2O2), xanthine oxidase has been found to catalyze sulfur trioxide anion radical (SO.-3) formation from sulfite anion (SO2-3). The SO.-3 radical was identified by ESR (electron spin resonance) spin trapping, utilizing 5,5-dimethyl-1-pyrroline-1-oxide (DMPO) as the spin trap. Inactivated xanthine oxidase does not catalyze SO.-3 radical formation, implying a specific role for this enzyme. The initial rate of SO.-3 radical formation increases linearly with xanthine oxidase concentration. Together, these observations indicate that the SO.-3 generation occurs enzymatically. These results suggest a new property of xanthine oxidase and perhaps also a significant step in the mechanism of sulfite toxicity in cellular systems.
| Idioma original | English |
|---|---|
| Páginas (desde-hasta) | 213-216 |
| Número de páginas | 4 |
| Publicación | FEBS Letters |
| Volumen | 303 |
| N.º | 2-3 |
| DOI | |
| Estado | Published - jun 1 1992 |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology