The enzymatic oxidation of Desferal to a nitroxide free radical

FEBS Lett. 1987 Oct 5;222(2):246-50. doi: 10.1016/0014-5793(87)80379-4.

Abstract

Desferrioxamine mesylate (Desferal), a transition metal ion chelator, has been used to inhibit the in vitro redox cycling of transition metal ions. ESR spectroscopy was utilized to detect and identify Desferal's one-electron oxidation product. We demonstrate that a horseradish peroxidase/H2O2 system, a xanthine oxidase/hypoxanthine system, and a hydroxyl radical-generating system are all capable of oxidizing Desferal to a nitroxide free radical. The same 9-line ESR spectrum (g = 2.0065, alpha N = 7.85 G, alpha H(2) = 6.35 G) was detected in all of the above systems. We, therefore, stress that care must be taken when using Desferal as a transition metal ion chelator to keep its concentration low enough to minimize these reactions, or to use a different metal ion chelator.

MeSH terms

  • Deferoxamine*
  • Electron Spin Resonance Spectroscopy
  • Horseradish Peroxidase
  • Hydrogen Peroxide
  • Hypoxanthine
  • Hypoxanthines
  • Nitrogen Oxides*
  • Oxidation-Reduction
  • Xanthine Oxidase

Substances

  • Hypoxanthines
  • Nitrogen Oxides
  • Hypoxanthine
  • Hydrogen Peroxide
  • Horseradish Peroxidase
  • Xanthine Oxidase
  • nitroxyl
  • Deferoxamine