Literature DB >> 1318848

Xanthine oxidase/hydrogen peroxide generates sulfur trioxide anion radical (SO3.-) from sulfite (SO3(2-)).

X Sun1, X Shi, N S Dalal.   

Abstract

In the presence of hydrogen peroxide (H2O2), xanthine oxidase has been found to catalyze sulfur trioxide anion radical (SO3.-) formation from sulfite anion (SO3(2-)). The SO3.- radical was identified by ESR (electron spin resonance) spin trapping, utilizing 5,5-dimethyl-l-pyrroline-l-oxide (DMPO) as the spin trap. Inactivated xanthine oxidase does not catalyze SO3.- radical formation, implying a specific role for this enzyme. The initial rate of SO3.- radical formation increases linearly with xanthine oxidase concentration. Together, these observations indicate that the SO3.- 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.

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Year:  1992        PMID: 1318848     DOI: 10.1016/0014-5793(92)80522-i

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  5 in total

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2.  Evaluation of the Forrester-Hepburn mechanism as an artifact source in ESR spin-trapping.

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Review 3.  Potential implication of the chemical properties and bioactivity of nitrone spin traps for therapeutics.

Authors:  Frederick A Villamena; Amlan Das; Kevin M Nash
Journal:  Future Med Chem       Date:  2012-06       Impact factor: 3.808

4.  New insights into the detection of sulfur trioxide anion radical by spin trapping: radical trapping versus nucleophilic addition.

Authors:  Kalina Ranguelova; Ronald P Mason
Journal:  Free Radic Biol Med       Date:  2009-04-09       Impact factor: 7.376

5.  In vitro evaluation of the potential role of sulfite radical in morphine-associated histamine release.

Authors:  Emma M Gordon; Carolyn Myers; Jeffrey Blumer
Journal:  BMC Pharmacol       Date:  2004-10-06
  5 in total

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