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"10.29235/1029-8940-2018-63-2-176-187vestib-362Research ArticleСтатьиТИАМИНАЗНАЯ АКТИВНОСТЬ ОКСОФЕРРИЛЬНЫХ ФОРМ МИОГЛОБИНАTHIAMINASE ACTIVITY OF MYOGLOBIN OXOFERRYL FORMSСтепуроИ. И.StepuroI. I.

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

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

scepura@gmail.comЛаборС. А.LaborS. A.

аспирант, мл. науч. сотрудник

Postgraduate student, Junior researcher

swet.labor2010@yandex.byШуриберкоА. В.ShuryberkaA. V.

аспирант, мл. науч. сотрудник

Postgraduate student, Junior researcher

the_chemistry@tut.byСтепуроВ. И.StsiapuraV. I.

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

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

stsiapura@gmail.comСмирновВ. Ю.SmirnovV. Yu.

ст. науч. сотрудник, доцент

Senior Researcher, Assistant Professor

vit_sm@mail.ruЯнцевичА. В.YantsevichA. V.

канд. хим. наук, заведующий лабораторией

Ph. D. (Chem.), Head of the Laboratory

Институт биохимии биологически активных соединений НАН Беларуси, ГродноInstitute of Biochemistry of Biologically Active Compounds of the National Academy of Sciences of Belarus, GrodnoГродненский государственный университет им. Я. Купалы, ГродноYanka Kupala State University of Grodno, GrodnoГродненский медицинский университет, ГродноGrodno State Medical University, GrodnoИнститут биоорганической химии НАН Беларуси, МинскInstitute of Bioorganic Chemistry of the National Academy of Sciences of Belarus, Minsk201821052018632176187Copyright © Степуро И.И., Лабор С.А., Шуриберко А.В., Степуро В.И., Смирнов В.Ю., Янцевич А.В., 20182018Степуро И.И., Лабор С.А., Шуриберко А.В., Степуро В.И., Смирнов В.Ю., Янцевич А.В.Stepuro I.I., Labor S.A., Shuryberka A.V., Stsiapura V.I., Smirnov V.Y., Yantsevich A.V.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/362

Окислительные превращения тиамина в присутствии метмиоглобина и пероксида водорода, в результате которых может образовываться ряд продуктов окисления, носят сложный характер. При инкубации тиамина с метмиоглобином и пероксидом водорода возможно расщепление молекулы тиамина по углероду метиленового мостика с образованием аминопиримидинового и тиазолового компонентов в виде отдельных молекул, а также образование тиохрома, тиаминдисульфида, оксодигидротиохрома, тиаминтиазолона. Окислительная трансформация фосфатов тиамина при инкубации с метмиоглобином и пероксидом водорода приводит к образованию аналогичных продуктов, однако в этом случае тиаминазная активность, т. е. расщепление на пиримидиновый компонент и фосфат тиазола, значительно выше. Добавление тирозина или парацетамола ингибирует тиаминазную активность, а также образование дисульфида тиамина, но увеличивает выход тиохрома или фосфатов тиохрома. С помощью спектрально-флуоресцентных методов, а также методов ВЭЖХ и масс-спектроскопии проведена идентификация продуктов окисления тиамина и фосфорных эфиров тиамина в пероксидазной реакции, катализируемой метмиоглобином в присутствии пероксида водорода. Обсуждается роль оксоферрильных форм миоглобина, образующихся при окислительном стрессе, в разрушении по тиаминазному пути тиаминдифосфата, который является коэнзимом важнейших ферментов энергетического метаболизма.

 

Thiamine oxidation chemistry in presence of metmyoglobin and hydrogen peroxide is quite complex and different products can be formed. Incubation of thiamine with metmyoglobin and hydrogen peroxide can result in splitting of thiamine molecule at carbon atom of the methylene bridge and production of aminopyrimidine and thiazole components as separate molecules or in formation of thiochrome, thiamine disulfide, oxodihydrothiochrome, and thiaminethiazolone. Oxidative transformation of thiamine phosphate esters in presence of metmyoglobin and hydrogen peroxide gives similar products however thiaminase activity, i.e. splitting of the molecules into aminopyrimidine and thiazole phosphate parts, is much higher in this case. Addition of tyrosine or paracetamol to incubation mixture inhibits thiaminase activity and formation of disulfides, but yield of thiochrome or thiochrome phosphates increases. Identification of products of thiamine (or its phosphate esters) oxidation in the presence of metmyoglobin and hydrogen peroxide was performed using HPLC, mass-spectrometry and spectral-fluorescent methods. Role of oxoferryl forms of myoglobin in degradation of thiaminediphosphate, cofactor of the important enzymes of carbohydrate metabolism, by thiaminase mechanism is discussed.

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