Abstract
Effects of thiamine and its derivatives on inhibition of dityrosine formation were studied in reactions catalyzed by oxoferryl forms of hemoglobin. At high thiamine concentrations, a complete inhibition of dityrosine formation was observed due to interaction of tyrosyl radicals with thiamine tricyclic and thiol forms. In neutral and alkaline media, tyrosyl radicals oxidized thiamine to thiochrome, oxodihydrothiochrome, and thiamine disulfide. In the absence of tyrosine, oxoferryl forms of hemoglobin manifested peroxidase activity towards thiamine and its phosphate esters by inducing their oxidation to disulfide compounds, thiochrome, oxodihydrothiochrome, and their phosphate esters, respectively, in neutral media. Thiamine and its phosphate esters were oxidized by both oxoferryl forms of hemoglobin, viz., +*Hb(IV=O) (compound I with an additional radical on the globin) and Hb(IV=O) (compound II). Putative mechanisms of thiamine conversions under oxidative stress and the protective role of hydrophobic thiamine metabolites are discussed.
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