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Oxidation of nitroxide radicals by an iron‐hydrogen peroxide‐amino acid system
Author(s) -
Yamaguchi Takeo,
Nagatoshi Akiyoshi,
Kimoto Eiji
Publication year - 1985
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(85)80120-4
Subject(s) - radical , chemistry , hydrogen peroxide , amino acid , tryptophan , nitroxide mediated radical polymerization , methionine , cysteine , tyrosine , hemoglobin , photochemistry , phenylalanine , methionine sulfoxide , hydroxyl radical , ferric , hemeprotein , heme , organic chemistry , biochemistry , enzyme , polymerization , radical polymerization , polymer
The oxidation of nitroxide radicals by the reaction of hemoglobin with hydrogen peroxide occurred using both FeSO 4 and amino acids instead of hemoglobin. Tyrosine, phenylalanine, tryptophan, methionine and cysteine in globin were connected with the formation of the oxoammonium cation. Of these amino acids, tyrosine was especially effective in its oxidation. It was found that both the binding of nitroxide radicals to ferric iron and the activation of amino acids by hydroxyl radicals were important in the radical oxidation.