Abstract
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.
Original language | English |
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Pages (from-to) | 213-216 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 303 |
Issue number | 2-3 |
DOIs | |
State | Published - Jun 1 1992 |
Keywords
- ESR
- Free radical
- Spintrapping
- Sulfite toxicity
- Sulfur trioxide anion radical
- Xanthine oxidase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology