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The enzymatic oxidation of Desferal to a nitroxide free radical
Author(s) -
Morehouse Kim.M.,
Flitter William D.,
Mason Ronald P.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80379-4
Subject(s) - chemistry , nitroxide mediated radical polymerization , hypoxanthine , chelation , oxidizing agent , xanthine oxidase , radical , transition metal , hydroxyl radical , horseradish peroxidase , metal ions in aqueous solution , redox , inorganic chemistry , photochemistry , metal , enzyme , organic chemistry , catalysis , radical polymerization , copolymer , polymer
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/H 2 O 2 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, a N = 7.85 G, a 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.