vestibИзвестия Национальной академии наук Беларуси. Серия биологических наукProceedings of the National Academy of Sciences of Belarus, Biological Series1029-89402524-230XThe Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"vestib-294Research ArticleСтатьиОКСОФЕРРИЛЬНЫЕ ФОРМЫ МИОГЛОБИНА И ГЕМОГЛОБИНА В ПРИСУТСТВИИ ФЕНОЛСОДЕРЖАЩИХ СОЕДИНЕНИЙ КАТАЛИЗИРУЮТ ОКИСЛИТЕЛЬНУЮ ТРАНСФОРМАЦИЮ ТИАМИНА И ЕГО ПРОИЗВОДНЫХIN THE PRESENCE OF PHENOL-CONTAINING COMPOUNDS OXOFERRYL FORMS OF MYOGLOBIN AND HEMOGLOBIN CATALYZE OXIDATIVE TRANSFORMATION OF THIAMINE AND ITS DERIVATIVESЛаборС. А.LaborS. A.

аспирант, мл. науч. сотрудник

Postgraduate student, Junior researcher

swet.labor2010@yandex.byСтепуроВ. И.StsiapuraV. I.

канд. физ.-мат. наук, вед. науч. сотрудник, доцент

Ph. D. (Phys. and Math.), Leading researcher, Assistant Professor

stsiapura@gmail.comСтепуроИ. И.StepuroI. I.

канд. биол. наук, вед. науч. сотрудник, доцент

Ph. D. (Biol.), Leading researcher, Assistant Professor

scepura@gmail.comСмирновВ. Ю.SmirnovV. Yu.

ст. науч. сотрудник, доцент

Senior Researcher, Assistant Professor

vit_sm@mail.ruИнститут биохимии биологически активных соединений НАН БеларусиInstitute of Biochemistry of Biologically Active Compounds of the National Academy of Sciences of BelarusГродненский государственный университет им. Янки КупалыYanka Kupala State University of GrodnoГродненский государственный медицинский университетGrodno State Medical University201704082017025565Copyright © Лабор С.А., Степуро В.И., Степуро И.И., Смирнов В.Ю., 20172017Лабор С.А., Степуро В.И., Степуро И.И., Смирнов В.Ю.Labor S.A., Stsiapura V.I., Stepuro I.I., Smirnov V.Y.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://vestibio.belnauka.by/jour/article/view/294

С помощью спектрально-флуоресцентных методов и метода высокоэффективной жидкостной хроматографии (ВЭЖХ) показано, что после инкубации тиамина с миоглобином и пероксидом водорода в водном растворе образуются тиохром, оксодигидротиохром и тиаминдисульфид. При добавлении тирозина или парацетамола в раствор метмиоглобина, пероксида водорода и тиамина резко повышается выход тиохрома, а выход оксодигидротиохрома и тиаминдисульфида снижается. В присутствии высоких концентраций парацетамола или тирозина тиамин превращается в тиохром, а выход оксодигидротиохрома и ти- аминдисульфида полностью ингибируется. Тиаминмонофосфат и тиаминдифосфат, в отличие от тиамина, стабильны и не окисляются даже после длительной инкубации в смеси с метмиоглобином и пероксидом водорода. Фосфорные эфиры тиамина не окисляются в соот- ветствующие фосфаты тиохрома в отсутствие монофенолов. Образование димеров тирозина, а также димеров и олигомеров парацетамола замедляется в присутствии тиамина и его фосфорных эфиров. Обсуждается механизм сопряженного окисления тиамина и его фосфорных эфиров с окислением монофенолов в пероксидазной реакции, катализируемой метмиоглобином и пероксидом водорода. 

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.

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The authors declare that there are no conflicts of interest present.