IN THE PRESENCE OF PHENOL-CONTAINING COMPOUNDS OXOFERRYL FORMS OF MYOGLOBIN AND HEMOGLOBIN CATALYZE OXIDATIVE TRANSFORMATION OF THIAMINE AND ITS DERIVATIVES

Using HPLC, absorption and fluorescence spectroscopy methods it was shown that incubation of thiamine with myoglobin and hydrogen peroxide in aqueous solution resulted in formation of thiochrome, oxodihydrothiochrome, and thiaminedisulfide. If tyrosine or paracetamol are present in incubation mixture besides metmyoglobin, hydrogen peroxide, and thiamine we observed significant growth of thiochrome yield and formation of oxodihydrothiochrome and thiaminedisulfide decreased. At high excesses of paracetamol or tyrosine the production of oxodihydrothiochrome and thiamine disulfide were inhibited and thiochrome was the only product of thiamine oxidation. In comparison to thiamine, its phosphate esters (thiamine monophosphate and thiamine diphosphate) are stable in presence of metmyoglobin and hydrogen peroxide and even prolonged times of incubation did not lead to their oxidative transformations. However, addition of monophenol compounds to the incubation mixture leads to oxidation of thiamine phosphate esters to the corresponding thiochrome phosphates. From the other side, formation of tyrosine dimers as well as paracetamol dimers and oligomers is lowered down in presence of thiamine and its phoshate esters. Mechanism of coupled oxidation of thiamine and its phosphate esters with oxidation of monophenols in peroxidase reaction catalyzed by metmyoglobin and hydrogen peroxide is discussed.

myoglobin, hemoglobin, hemoprotein, oxoferryl form, ferri-form, oxodihydrothiochrome, thiaminedisulfide, tiochrome, metmyoglobin, methemoglobin, tyrosine radicals, tiaminpirofosfat, thiamin diphosphate

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