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The interaction of alcohol peroxyl radicals with human oxyhemoglobin
Author(s) -
SzwedaLewandowska Z.,
Krokosz A.,
Zajaczkowska W.,
Puchaŀa M.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202032
Subject(s) - radical , chemistry , photochemistry , oxidizing agent , alcohol , ethanol , tryptophan , butanol , organic chemistry , biochemistry , amino acid
The effects of interaction of ethanol, l‐butanol or t‐butanol peroxyl radicals with oxyhemoglobin (HbO2) were estimated using absorption spectroscopy in the visible range and tryptophan fluorescence. Peroxyl radicals were generated by gamma‐radiation. Alcohol peroxyl radicals showed the same effectiveness in oxidizing HbO2 iron as ‐OH radicals (GFe(III) = 1.8 for a dose 0.33 kGy). However, they degraded hemoglobin to hemichromes and cholehemichromes to a lesser degree than ‐OH radicals. In addition l‐ and t‐butanol peroxyl radicals were less effective than peroxyl ethanol radicals. Alcohol peroxyl radicals caused unfolding of protein to a much lesser degree than ‐OH radicals. Their contribution to the destruction of tryptophan residues was nearly matched by those obtained with the ‐OH radicals.