Head of Laboratory
Natalya Nikolaevna UGAROVA, Professor, D.Sc.(Chemistry).

Address for correspondence:
Department of Chemical Enzymology, Faculty of Chemistry,
The M.V.Lomonosov Moscow State Univeristy,
119899 Moscow GSP-3, Russian Federation
Tel. +7(095) 939-26-60, 939-26-52, Fax: +7(095) 939-54-17,

  • The Laboratory was found in 1980 on the initiative of Professor I.V.Berezin, the corresponding member of the Russian Academy of Science, who was the dean of Chemistry Department at that time. From the beginning Prof. N.N.Ugarova is the head of this laboratory..
  • 25 researchers, engineers and technicians are on the staff of the Laboratory. They are devided into several separate scientific groups. Professor N.N.Ugarova is general supervisor of the staff and a leader of one of the scientific groups involved into the studies of physicochemical basics of energy bioconversion.
  • Professor N.N.Ugarova is general supervisor of the staff and a leader of one of the scientific groups involved into the studies of physicochemical basis of energy bioconversion.

The group of Prof. N. Ugarova consists of 8 scientific researchers, 3 engineers, graduate student, master’s student, undergraduate students.
Name  Position, scientific degree  E-mail address
Natalya Nikolaevna Ugarova  Head of Laboratory, Doctor of Science
Lubov Yulievna Brovko  Principal researcher, Doctor of Science  .
Ekaterina Igorevna Dementieva  Senior reseacher, Ph.D. in Chemistry
Nadejda Anatolievna Romanova  Researcher, Ph.D. in Biology .
Olga Vladimirovna Leontieva Researcher, Ph.D. in Chemistry
Olga Vladimirovna Lebedeva Researcher, Ph.D. in Chemistry .
Valeriy Gaikovich Froundjiyan Researcher
Irina Alexandrovna Lundovskich Researcher
Elena Alexandrovna Chudinova Postgraduate Student

Principal results earlier obtained:

Topic:  "Biocatalysis by peroxidase and construction of peroxidase-based bioanalytical systems"
 Principal results:
- The mechanism of dissociation and reconstruction of heme-protein complex of peroxidase is elucidated. - The methods of peroxidase stabilization in solution and in immobilized state are developed using chemical modification and/or optimization of the enzyme microenvironment.
 - Inhibitory effect of different physiologically active substances and drugs on peroxidase is studied. The methods of these substances’s assay are elaborated using peroxidase.


"Physicochemical basis of energy bioconversion in bioluminescent systems and development of bioluminescent express-assays for medicine, ecology, technology and scientific studies"
Principal results:
- Kinetics and mechanism of firefly luciferase reaction have been elucidated.
- The luciferase monomer-dimer interactions is shown to play an important role in the catalysis and enzyme stabilization.
- Inactivation of luciferase is the main cause of the decrease in bioluminescence intensity during luciferase functioning.
- Methods of luciferase stabilization and immobilization were developed.

Principal results recently obtained and main trends of present investigations:

Under investigation:
Under investigation:

Principal directions of the applied studies of the laboratory:

  1. The development of the reagents for ATP assay using soluble or immobilized recombinant luciferase.
  2. Optimization of the "rapid microbiology" methods for control of microbial contaminations in food, water, biological samples (blood, wounds, etc.), technological materials and development of assays for overall microbial contaminations and specific strains.

Selected publications

  1. N.N.Ugarova, L.Yu.Brovko, and G.D.Kutuzova (1993) Bioluminescence and bioluminescent analysis: recent development in the field (review) Biochemistry (Moscow), 58, 976-992.
  2. J.H.Devine, G.D.Kutuzova, V.A.Green, N.N.Ugarova, and T.O.Baldwin (1993) Luciferase from east european firefly Luciola  mingrelica: cloning and nucleotide sequence of the cDNA, overexpression in Esherichia  coli and purification of the enzyme. Biochim.Biophys.Acta, 1173, 121-132.
  3. L.Yu. Brovko, N.A.Romanova, and N.N.Ugarova (1994) Bioluminescent assay of bacterial intracellular AMP, ADP, and ATP with the use of a coimmobilized three-enzyme reagent (adenylate kinase, pyruvate kinase, and firefly luciferase). Anal. Biochem., 220, 410-414.
  4. O.A.Gandelman, L.Yu. Brovko, A.Yu. Chikishev, A.P.Shkurinov, and N.N.Ugarova, (1994) Investigation of the interaction between firefly luciferase and oxyluciferin or its analogues by steady state and subnanosecond time-resolved fluorescence. J. Photochem. Photobiol. B: Biol., 22, 203-209.
  5. L.Yu.Brovko, O.A.Gandelman, T.E.Polenova, and N.N.Ugarova, (1994) Kinetics of bioluminescence in the firefly luciferin-luciferase system. Biochemistry (Moscow), 59, 195-201.
  6. E.G.Bulanova, V.M.Budagyan, N.A.Romanova, L.Yu.Brovko, and N.N.Ugarova (1995) Bioluminescent assay for human lymphocyte blast transformation. Immonology Lett. 46, 153-155
  7. E.I.Dementieva, E.E.Zheleznova, G.D.Kutuzova, I.A.Lundovskikh, and N.N.Ugarova (1996) Physicochemical properties of recombinant Luciola mingrelica luciferase and its mutant forms. Biochemistry (Moscow) 61, N1, 115-119.
  8. I.A.Lundovskikh, E.I.Dementieva, and N.N.Ugarova (1998) Immobilization of recombinant firefly luciferase. Physicochemical properties and application. Biochemistry (Moscow), 63, N 6,  691-696.
  9.  N.N.Ugarova, L.Yu.Brovko, and E.I.Dementieva (1998) Bioluminescence and Chemiluminescence.In: Luminescence of Solids. D.R.Vij, ed. Plenum Press, N.Y., London, 391-411.

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Last updated in May 6, 2003

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