Chair: Sergey B. Bokut,
PhD (biology), assistant professor

Tel: +(375 17) 230 39 39

The Department of Biochemistry and Biophysics trains specialists on the specialization  "Medical-biological business " 1-80 02 01 with specialization "Biochemistry" and qualification awarding "biologist-analyst"

Disciplines:

• General and inorganic chemistry 
• Analytical chemistry
• Organic chemistry
• General biochemistry
• General and environmental biochemistry
• Physical and colloid chemistry
• Medical and biological physics – section: Medical physics
• Medical and biological physics – section: Biological physics
• Grand special course: chemical – analytical methods in biology – section: High-performance liquid chromatography in biology
• Molecular biology and genetic engineering
• Molecular biology of viruses and antiviral therapy
• Molecular biology of viruses
• Pathobiochemistry
• Laboratory diagnostics 
• Methods of clinical biochemistry
• Methods of clinical biophysics
• Biotechnology
• Methods of physico-chemical biology in study of structural-functional protein function
• Chemistry and biochemistry of carbohydrates
• Chemistry of natural and synthetic lipids

Academic laboratories

• Physical chemistry
• General and inorganic chemistry

Research Laboratory

• Radiation biochemistry and biophysics

Research Directions:

• The molecular markers of negative ecological factors effect on human organism.
• The structure-functional properties of minor human hemoglobin forms under the influence of aggressive ecological factors.
• The interrelation between the structure-conformational and functional properties of glycosylated minor human hemoglobin forms.
• The investigation of crystallization conditions of main and minor human hemoglobin forms at its different conformational states.
• The investigation of the potential possibility of oxygen recombination to human hemalbumine.

Scientific Results:

• Binding of 1,8-anilinonaphthalene sulfonate (1,8-ANS) to main (HbA1) and glycosylated (HbA1C) forms of human oxyhemoglobin in the presence/absence of inositolhexaphosphate (IHP was studied by time-correlated single photon counter with subnanosecond time resolution. The redistribution of contributions of the most long-lived and the most short-lived fluorescent decay components in the presence of IHP provide an evidence of the probe binding within oxyhemoglobin central cavity, namely DPG-binding site. Finally, it was shown that the fluorescent probe is extremely sensitive for hemoglobin central cavity modification, provided by the carbohydrate moiety in case of 1,8-ANS interactions with HbA1C.
• The investiation of 1,8-ANS binding to glycosylated form of human oxyhemoglobin (HbA1C) showed that the fluorescent probe is extremely sensitive for hemoglobin central cavity modification, provided by the carbohydrate moiety in case of 1,8-ANS interactions with HbA1C.
• The preparative isolation procedure of minor glycosylated hemoglobin forms was developed. Electrospray ionization mass spectrometry was then used to characterize HbÀ1Ñ glycosylation nature. The single HbA1C peak was divided into several fractions that were analyzed independently.
• The bimolecular stage of recombination of Hb (HbA1, HbA1c, HbA1b) and O2 obtained by nanosecond laser flash-photolysis in the presence/absent of IHP was investigated. The results show that oxygen recombination kinetics are described by two processes with different characteristic times and Hb-form–dependent contributions. Alteration of the processes contributions observed in HbA1C in comparison with HbA1 suggests an existence of long-range interactions between the hemoglobin central cavity and the a- and b subunits heme proximity. In comparison with HbA1C, unknown modification in the HbA1b leads to the most markable effect on oxygen rebinding. This effect is similar to that of the IHP addition to HbA1.
• The effect hemoglobin glycosylation is to block the hemoglobin conformation in the R and R2 state by steric hindrance to the deoxy T state. The superposition of T state (2hhb.pdb) against the glycated tetramer and the glucose in the switch region shows clearly that the presence of this covalently linked Amadori product is giving steric hindrance to the Helix G of the T state tetramer. The increase lifetime of the oxygenated R state of hemoglobin will increase the probability of a nucleophilic attack of a water molecule that displace the bound dioxygen from HbO2 in the form of O2•. The consequences of theses structural changes is the increasing in the oxidation rate to the ferric met-form of hemoglobin leading to higher level of O2• causing oxidative stress.

Partners:

Collaboration with organizations of the Republic of Belarus:

• B.I. Stepanov Institute of Physics of the National Academy of Sciences of Belarus.
• Institute of Molecular and Atomic Physics of the National Academy of Sciences of Belarus.
• Institute of the Bioorganic Chemistry of the National Academy of Science of Belarus .
• Institute of Microbiology of the National Academy of Science of Belarus.

International collaboration:

• Institut de Genetique et de Bioloqie Moleculaire et Cellulaire (IGBMC), Illkirsch, France:
  • Laboratore de bioloqie et genomique structurales,
  • Departement: Genetique physiologique and signalisation nucleaire.
• Universite Louis Pasteur (Strasbourg I), Strasbourg, France.

Publications:

1. Parul D. A., Bokut S. B., Kisselev P.A., Milyutin A. A., Petrov E. P., Nemkovich N. A., Sobchuk A. N., Dzhagarov B. M. Fluorescence decay time distribution analysis reveals two types of binding sites for 1,8-anilinonaphthalene sulfonate in native human oxyhemoglobin, Biochemistry , 2002, Vol. 66, ¹4, 390-396.
2. Syakhovich V.E., Parul D.A., Ruta E.Ya., Bushuk B.A., Bokut S.B. 1,8-Anilinonaphthalene sulfonate binds to central cavity of human hemoglobin, Biochem. Biophys. Res. Commun. , Vol. 317, 2004, 761-767.
3. Kisselev P., Schunck W.H., Roots I., Schwarz D., Association of CYP1A1 polymorphisms with differential metabolic activation of 17beta-estradiol and estrone, Cancer Res. , 2005, 65, ¹7, 2972-2978.
4. Schwarz D., Kisselev P., Chernogolov A., Schunk W.H., Roots I. Human CYP1A1 variants lead to different eicosapentaenoic acid metabolite pattern, Biochem. Biophys. Res. Commun. , 2005, 336 (3), 779-783.
5. Syakhovich V.E., Bokut S.B. Full separation, mass spectrometry and inhibitory analysis of human hemoglobin A 1C , 6 th International scientific conference Sakharov readings 2006: environmental problems of the XXI century, May 18-19, Minsk , Belarus . ISEU, Minsk , Bestprint, 2006, part I, p. 75-83.
6. Syakhovich V.E., Saraswathi N.T., Ruff M., Bokut S.B., Moras D., Crystallization and preliminary crystallographic analysis of human glycosylated hemoglobin, Acta Cryst. F: Struct. Biol. Cryst . Commun . , 2006, F62 (2) 106-109 .
7. Bushuk S.B., Bokut S.B., Kalvinkovskaya Ju.A., Stanevich V.V., Zinchenko A.I., Titovich O.I., Bushuk B.A., Interaction of doxorubicin with yeast DNA and RNA modelling polynucleotides, ICONO- lat, 2007, Technical Digest , I07-2
8. Bushuk S.B., Bokut S.B., Kalvinkovskaya Ju.A., Kisel M.A., Bushuk B.A., Adriamycin steady - state and time - resolved spectroscopic properties in liposomes of various composition, ICONO- lat, 2007, Technical Digest , I07-3
9. Birichevskaya L . L ., Kvach S . V ., Sivets G . G ., Kalinichenko E . N ., Zinchenko A . I . , Mikhailopulo I . A . A comparison of enzymatic phosphorylation and phosphatidylation of b - L - and b - D -nucleosides // Biotechnology Letters . – 2007. – V. 29, N 4. – P. 585–591.
10. Saraswathi N.T., Syakhovich V.E., Bokut S.B., Moras D., Ruff M. The effect of hemoglobin glycosylation on diabetes linked oxidative stress, Pdb3b75/pdb , release 2008-10-14.
11. Burko, D.V. Application of Escherichia coli recombinant Lysyl-tRNA
    synthetase for the synthesis of diadenosine 5 / ,5 /// -Pl,P4-tetraphosphate / D.V. Burko, S.V.
    Kvach, A.L Zinchenko // Biotechnology: State of the Art and Prospects for Development
    / Ed. G.E. Zaikov. – NY: Nova Science Publishers, Inc. – 2008. – P. 31-37.
12. Compensation of DNA stabilization and destabilization effects caused by cisplatin is partially disturbed in alkaline medium / E.N. Galyuk, M.M Hauruk , D.Y. Lando // J. Biomol. Struct. Dynam. , 2008, V. 25, ¹4, P. 407-417.
13. P yrko A.N., Synthesis and transformations of new derivatives 1,2,3,4,5,6,7,8,9,10-decahydroacridine-1,8-diones, Russian J. Org. Chem . – 2008. – V . 44, N 8. – 1215-1224.
14. Dieter Schwarz, Pyotr Kisselev, Wolf-Hagen Schunck, Ivar Roots, Inhibitionof 17ß-estradiol activation by CYP1A1: Genotype- and regioselective inhibition by St. John´s wort and several natural polyphenols , Biochem. Biophys. Res. Commun . 2009, in press
15. Saraswathi N.T., Syakhovich V.E., Bokut S.B., Moras D., Ruff M. Crystal structure of glycated human haemoglobin, Pdb3b75/pdb , last modified 2009-02-24.
16. Saraswathi N.T., Syakhovich V.E., Bokut S.B., Moras D., Ruff M. The effect of hemoglobin glycosylation on diabetes linked oxidative stress: crystal structure of glycated human haemoglobin, Biochemistry ( Moscow ), 2009, in press.
17. Birichevskaya L.L., Titovich O.I., Kisel M.A., Zinchenko A.I. Application of Streptomyces netropsis phospholipase D for synthesis of phosphatidylserine. Biotechnology, Biodegradation, Water and Foodstuffs / Eds. G.E. Zaikov and L.P. Krylova.-NY: Nova Science Publishers, Inc. – 2009. – P. 65–71.

Faculty:

Name, Family Name	Scientific Degree, Academic Degree, Position	Disciplines	E-mail
Sergey B. Bokut	Ph.D. (Biology) Associate Professor Chair	Molecular biology and genetic engineering Pathobiochemistry
Vitaly E. Syakhovich	Senior lecturer Deputy Head of Chair	General Biochemistry General and Environmental Biochemistry
Anatoly I. Zinchenko	Dr.Sc. (Biology) Professor, Corresponding Member of NAS Belarus	Biotechnology Molecular biology of Viruses and Antiviral therapy
Peter A. Kisselev	Dr.Sc. (Chemistry) Professor	Physical and Colloid Chemistry
Evgeny I. Kvasyuk	Dr.Sc. (Chemistry) Professor	Organic Chemistry Structure biology methods in study of proteins function Chemistry and biochemistry of carbohydrates
Aleksey K. Baev	Dr.Sc. (Chemistry) Professor	General & Inorganic Chemistry Analytical Chemistry
Ludmila M. Shejko	Ph.D. (Biophysics) Associate Professor	Biophysics
Michail V. Baikou	Ph.D. (Chemistry) Senior lecturer	General & Inorganic Chemistry
Georg M. Kostin	Ph.D. (Medicine) Associate Professor	Medicine Physics
Nikolai A. Zhernosek	Ph.D. (Biology) Associate Professor	Laboratory Diagnostics Methods of Clinical Biochemistry Methods of Clinical Biophysics
Ludmila L. Avdei	Ph.D. (Medicine) Associate Professor	Medicine Physics
Klavdziya Ya. Bulanava	Ph.D. (Biology) Associate Professor	Chemistry of natural and synthetic lipids
Svetlana V. Kobyasheva	Senior lecturer	Organic Chemistry
Liudmila F. Padabed	Lecturer	General & Inorganic Chemistry Analytical Chemistry
Evgenia A. Dokuchaeva	Lecturer	General Biochemistry Molecular Biology and Genetic Engineering
Natalia V. Bogdanova		General and Environmental Biochemistry Pathobiochemistry
Svetlana V. Lyakh	Lecturer	Laboratory Diagnostics
Ekaterina I. Tarun	Ph.D. (Chemistry) Associate Professor	General & Inorganic Chemistry Organic ChemistryPhysical and Colloid Chemistry
Nina S. Kuprina	Lecturer	General & Inorganic Chemistry Organic Chemistry