LABORATORY FOR PHYSICO-CHEMICAL
BASICS OF ENERGY BIOCONVERSION
Head of Laboratory
Natalya Nikolaevna UGAROVA,
Address for correspondence:
of Chemical Enzymology, Faculty of Chemistry,
Moscow State Univeristy,
GSP-3, Russian Federation
939-26-60, 939-26-52, Fax: +7(095) 939-54-17, E-mail:firstname.lastname@example.org
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,
|| 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
|Irina Alexandrovna Lundovskich
|Elena Alexandrovna Chudinova
Principal results earlier obtained:
||"Biocatalysis by peroxidase and construction
of peroxidase-based bioanalytical systems"
- 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"
- 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
Principal results recently obtained
and main trends of present investigations:
Hypothesis was proposed to explain the observed shifts
in bioluminescence spectra for different firefly luciferases. According
to this hypothesis, substitution of the aminoacid residues in the emitter
microenvironment changes polarizability of the medium and causes the bioluminescence
The dissociative mechanism of bioluminescence
was proposed, i.e. chemiexcitation causes dissociation of the enzyme-chromophore
complex and electronically excited product rebinds with the enzyme after
Photoinduced dynamics of bioluminescent luciferin-luciferase
system using picosecond laser spectroscopy to elucidate the role of conservative
Trp residue in this process.
Genetic engeneering studies of firefly luciferase
were developed: gene of Luciola mingrelica luciferase was cloned, kinetics
of gene expression in E.coli cells showed the important role of ATP and
DnaK chaperone in luciferase folding, the plasmid-superproducer pLR was
constructed, the role of some aminoacid residues in activity and stability
of luciferase was elucidated using site-specific mutagenesis.
Studies of luciferase active site using site-mutagenegis
and computer modeling of the enzyme.
Principal directions of the applied
studies of the laboratory:
The development of the reagents for ATP assay using
soluble or immobilized recombinant luciferase.
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.
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.
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,
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.
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.
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.
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
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,
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.
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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