Xanthine oxidase/hydrogen peroxide generates sulfur trioxide anion radical (SO.-3) from sulfite (SO2-3)

  • Xiaoya Sun
  • , Xianglin Shi
  • , N. S. Dalal

Producción científica: Articlerevisión exhaustiva

23 Citas (Scopus)

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 originalEnglish
Páginas (desde-hasta)213-216
Número de páginas4
PublicaciónFEBS Letters
Volumen303
N.º2-3
DOI
EstadoPublished - jun 1 1992

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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