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Синтез резервных полигидроксиалканоатов светящимися бактериями [Текст] : научное издание / А. Н. Бояндин [и др.] // Микробиология. - 2008. - Т. 77, N 3. - С. 364-369 . - ISSN 0026-3656

ГРНТИ

34.27.17

Рубрики:
ПОЛИГИДРОКСИАЛКАНОАТЫ
   РЕЗЕРВНЫЕ
   БИОСИНТЕЗ
   СВЕТЯЩИЕСЯ БАКТЕРИИ
   МОРСКИЕ
   PHOTOBACTERIUM LEIOGNATHI (BACT.)
   PHOTOBACTERIUM PHOSPHOSEUM (BACT.)
   VIBRIO HARVEYI (BACT.)
   VIBRIO FISCHERI (BACT.)
   ВЫДЕЛЕНИЕ
Аннотация: Исследована способность морских светящихся бактерий синтезировать в кач-ве резервных макромолекул полиэфиры гидроксикарбоновых к-т (полигидроксиалканоаты, ПГА). Проанализировано 20 штаммов из коллекции светящихся бактерий CCIBSO (WDCM836) Ин-та биофизики СО РАН, относящихся к различным таксонам (Photobacterium leiognathi, Ph. phosphoreum, Vibrio harveyi, V. fischeri). Выделены наиболее продуктивные штаммы, и определены условия, обеспечивающие высокие выходы полимера в периодической культуре (40-70% к весу сухого в-ва клетки). Обнаружена способность представителей Ph. leiognathi и V. harveyi синтезировать двух- и трехкомпонентные полимеры, содержащие в кач-ве основного мономера гидроксимасляную к-ту и в кач-ве минорных - гидроксивалериановую и гидроксигексановую к-ты. Результаты позволяют рассматривать светящиеся микроорганизмы в кач-ве новых продуцентов многокомпонентных полигидроксиалканоатов. Россия, Ин-т биофизики СО РАН, Красноярск. E-mail: araneus@mail.ru. Библ. 22

Держатели документа:
Институт биофизики СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бояндин, А.Н.; Калачева, Г.С.; Родичева, Э.К.; Волова, Т.Г.

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^a341.27.53.07^2VINITI
Г 51

Гительзон, И. И.
Светящиеся бактерии, ассоциированные с бентосными организмами [Текст] : научное издание / И. И. Гительзон, Т. И. Воробьева // Микробиология. - 1988. - Т. 57, N 5. - С. 847-852

ГРНТИ

34.27.53

РУБ 341.27.53.07
Рубрики:
СВЕТЯЩИЕСЯ БАКТЕРИИ
   VIBRIO HARVEYI (BACT.)
   PHOTOBACTERIUM (BACT.)
   ВСТРЕЧАЕМОСТЬ
   БЕНТОСНЫЕ ЖИВОТНЫЕ
   КИШЕЧНИК ДОННЫХ ЖИВОТНЫХ
   ВОДНЫЕ ЭКОСИСТЕМЫ
   ИНДИЙСКИЙ ОКЕАН
   КОРАЛЛОВЫЕ РИФЫ
Аннотация: Исследована встречаемость светящихся бактерий в ассоциации с бентосными животными, в частности, обитателями коралловых рифов. Обнаружено, что светящиеся бактерии регулярно встречаются на поверхности тела и в кишечнике многих донных животных, но ни с одним из обследованных видов не связаны облигатно. Их ареал простирается от литорали до максимально обследованных глубин 1600 м. Определен состав выделенных бактерий, доминирующим оказался вид Vibrio harveyi, в отличие от морских рыб, кишечник к-рых населен преимущественно видами р. Photobacterium.

Доп.точки доступа:
Воробьева, Т.И.

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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria [Text] / V. N. Petushkov [et al.] // J. Phys. Chem. B. - 2003. - Vol. 107, Is. 39. - P. 10934-10939, DOI 10.1021/jp034266e. - Cited References: 52 . - ISSN 1520-6106

РУБ Chemistry, Physical
Рубрики:
TIME-RESOLVED FLUORESCENCE
   VIBRIO-FISCHERI Y1
   FEMTOSECOND SOLVATION DYNAMICS
   FLAVIN ADENINE-DINUCLEOTIDE
   PHOTOBACTERIUM-LEIOGNATHI
   BIOLOGICAL WATER
   SOLVENT DYNAMICS
   DIELECTRIC-RELAXATION
   MOLECULAR-DYNAMICS
   TRYPTOPHAN
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by similar to7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

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Держатели документа:
Univ Wageningen & Res Ctr, Biochem & Biophys Lab, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
Vrije Univ Amsterdam, Fac Sci & Engn, Dept Phys & Astron, NL-1081 HV Amsterdam, Netherlands
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Vrije Univ Amsterdam, Fac Earth & Life Sci, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; van Stokkum, IHM; Gobets, B...; van Mourik, F...; Lee, J...; van Grondelle, R...; Visser, AJWG

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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria / V. N. Petushkov [et al.] // Journal of Physical Chemistry B. - 2003. - Vol. 107, Is. 39. - P10934-10939 . - ISSN 1520-6106
Кл.слова (ненормированные):
Bacteria -- Bioluminescence -- Chemical relaxation -- Chromophores -- Dielectric properties -- Proteins -- Solvents -- Bioluminescent bacteria -- Dimethyl ribityl lumazine -- Photobacterium leiognathi -- Riboflavin -- Ultrafast fluorescence relaxation spectroscopy -- Fluorescence
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by ?7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

Scopus
Держатели документа:
MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, Netherlands
Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, Netherlands
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States
Department of Structural Biology, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk 660036, Russian Federation
IPMC, Universite de Lausanne, CH 1015 Lausanne, Switzerland : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Van Stokkum, I.H.M.; Gobets, B.; Van Mourik, F.; Lee, J.; Van Grondelle, R.; Visser, A.J.W.G.

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Transfer of xenobiotics through cell membranes of luminous bacteria / S. E. Medvedeva // Luminescence. - 1999. - Vol. 14, Is. 5. - P267-270 . - ISSN 1522-7235
Кл.слова (ненормированные):
Luminous bacteria -- Toxicant -- Ultrastructure -- bacterial DNA -- edetic acid -- toluene -- xenobiotic agent -- article -- cell membrane -- DNA damage -- drug effect -- luminescence -- metabolism -- Photobacterium -- sensitivity and specificity -- transport at the cellular level -- ultrastructure -- Vibrio -- Biological Transport -- Cell Membrane -- DNA Damage -- DNA, Bacterial -- Edetic Acid -- Luminescence -- Photobacterium -- Sensitivity and Specificity -- Toluene -- Vibrio -- Xenobiotics
Аннотация: The influence of some chemical substances on luminous bacteria was studied to elucidate the interrelation between the xenobiotics action on bacterial luminescence and cell ultrastructure. Such substances as quinones, phenols, chlorides of heavy metals (in concentrations of substances inhibiting luminescence by 50%) resulted in damaging effects upon bacteria: a lot of cells had damage of membranes due to changes in their permeability. It was found that the high concentration of EDTA and toluene decreased the luminescence and caused the condensation of DNA-fibrils and the cell damage after long-term and short-term action. The low concentration of EDTA and toluene did not decrease the bacterial luminescence; the noticeable damage of cell membranes did not take place during short-term treatment. However, the long action of these substances changed the membrane permeability resulting in increased sensitivity of bacterial luminescence to some toxic substances. Copyright В© 1999 John Wiley & Sons, Ltd.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Medvedeva, S.E.

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The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - P774-779, DOI 10.1006/bbrc.1995.1880 . - ISSN 0006-291X
Кл.слова (ненормированные):
riboflavin -- article -- bioluminescence -- fluorescence -- nonhuman -- priority journal -- protein analysis -- protein synthesis -- vibrio -- vibrionaceae -- Bacterial Proteins -- Chromatography, Gel -- Chromatography, Thin Layer -- Flavin Mononucleotide -- Flavoproteins -- Luminescence -- Riboflavin -- Spectrometry, Fluorescence -- Support, U.S. Gov't, P.H.S. -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Vibrio -- Vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

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Synthesis of reserve polyhydroxyalkanoates by luminescent bacteria / A. N. Boyandin [et al.] // Microbiology. - 2008. - Vol. 77, Is. 3. - P318-323, DOI 10.1134/S0026261708030119 . - ISSN 0026-2617
Кл.слова (ненормированные):
Biosynthesis -- Chemical structure -- Luminescent bacteria -- Polyhydroxyalkanoates (PHA) -- Bacteria (microorganisms) -- Photobacterium leiognathi -- Vibrio harveyi
Аннотация: The ability of marine luminescent bacteria to synthesize polyesters of hydroxycarboxylic acids (polyhydroxyalkanoates, PHA) as reserve macromolecules was studied. Twenty strains from the collection of the luminescent bacteria CCIBSO (WDCM839) of the Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, assigned to different taxa (Photobacterium leiognathi, Ph. phosphoreum, Vibrio harveyi, and V. fischeri) were analyzed. The most productive strains were identified, and the conditions ensuring high polymer yields in batch culture (40-70% of the cell dry mass weight) were determined. The capacity for synthesizing two-and three-component polymers containing hydroxybutyric acid as the main monomer and hydroxyvaleric and hydroxyhexanoic acids was revealed in Ph. leiognathi and V. harveyi strains. The results allow luminescent microorganisms to be regarded as new producers of multicomponent polyhydroxyalkanoates. В© 2008 MAIK Nauka.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A.N.; Kalacheva, G.S.; Rodicheva, E.K.; Volova, T.G.

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Structural transitions of photobacterium leiognathi luciferase determined by various optical techniques under urea-induced equilibrium denaturation / D. V. Gulnov [и др.] // Tsitologiya. - 2018. - Vol. 60, Is. 10. - С. 847-850, DOI 10.7868/S0041377118100181 . - ISSN 0041-3771
Кл.слова (ненормированные):
Bacterial luciferase -- Circular dichroism -- Denaturation -- Protein fluorescence lifetime -- Protein intermediate states
Аннотация: The study was aimed to identification of conformational transitions of Photobacterium leiognathi luciferase during equilibrium denaturation with urea using several optical techniques, including circular dichroism, stationary and time-resolved fluorescence. Gravity center and intensity ratio I 325 /I 390 for the fluorescence spectra, molar ellipticity at 222 nm and fluorescence lifetimes of the protein were analyzed. Investigated parameters revealed two possible transitions for P. leiognathi luciferase with the midpoints at 0.5—1.1 and 3.5—4.2 M of urea. Changes in the values of two lifetime components, characterizing the luciferase fluorescence reflect both transitions, while steady-state fluorescence parameters (gravity center of spectrum and I 325 /I 390 ratio) reveal only the second one. Far-UV circular dichroism spectra displayed transitions at 4.2 M of urea for P. leiognathi luciferase. Conformational transitions characteristics of P. leiognathi luciferase and previously studied Vibrio harveyi luciferase (Inlow et al., 2002) were compared. Since, according to the published data for V. harveyi, midpoint of the second conformational transition is at about 2.5 M of urea, the results indicate more stable secondary structure for the P. leiognathi luciferase under study. The possible reasons for observed differences in fluorescent characteristics of two types of luciferases during denaturation can be connected to the microenvironment variation of the tryptophan residues in their tertiary structure, namely in position 131 and 277 in a-subunit. © 2018 Sankt Peterburg. All rights reserved.

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Смотреть статью
Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Gulnov, D. V.; Nemtseva, E. V.; Gerasimova, M. A.; Kratasyuk, V. A.

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Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria [Text] / V. N. Petrushkov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P. 164-180. - Cited References: 18 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
YELLOW FLUORESCENT PROTEIN
   FISCHERI STRAIN Y-1
   AMINO-ACID-SEQUENCE
   VIBRIO-FISCHERI
   PHOTOBACTERIUM-LEIOGNATHI
   RIBOFLAVIN PROTEIN
   LUMINOUS BACTERIUM
   LUMAZINE PROTEIN
   FMN
   Y1

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Agr Univ Wageningen, Dept Biochem, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petrushkov, V.N.; Gibson, B.G.; Visser, AJWG; Lee, J...

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10.

Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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11.

Protein-protein complexation in bioluminescence [Text] / M. S. Titushin [et al.] // Protein Cell. - 2011. - Vol. 2, Is. 12. - P957-972, DOI 10.1007/s13238-011-1118-y. - Cited References: 114. - The work was funded by "Fellowship for Young International Scientists" of Chinese Academy of Sciences. This work was supported by the National Natural Science Foundation of China (Grant Nos: 30870483, 31070660, 31021062 and 81072449), Ministry of Science and Technology of China (Nos. 2009DFB30310, 2009CB918803 and 2011CB911103), CAS Research Grants (Nos. YZ200839 and KSCX2-EW-J-3). . - ISSN 1674-800X

РУБ Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
   LUCIFERIN-BINDING-PROTEIN
   RENILLA-RENIFORMIS LUCIFERASE
   VIBRIO-FISCHERI Y1
   JELLYFISH CLYTIA-GREGARIA
   ALPHA/BETA-HYDROLASE FOLD
   AMINO-ACID-SEQUENCE
   BACTERIAL LUCIFERASE
   ENERGY-TRANSFER
   CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
green-fluorescent protein (GFP) -- photoprotein -- luciferase -- lumazine protein -- Forster resonance energy transfer (FRET) -- docking
Аннотация: In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca2+-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of X-ray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

Держатели документа:
[Titushin, Maxim S.
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Feng, Yingang] Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Feng, Y.G.; Lee, J...; Vysotski, E.S.; Liu, Z.J.

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12.

PROSPECTS FOR APPLICATION OF BIOLUMINESCENCE METHOD IN MEDICINE [Текст] / I. I. GITELZON, T. P. SANDALOVA // VESTNIK AKADEMII MEDITSINSKIKH NAUK SSSR. - 1990. - Is. 9. - С. 31-35. - Cited References: 41 . - ISSN 0002-3027

РУБ Medicine, General & Internal
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   VIBRIO-HARVEYI
   BACTERIAL LUCIFERASE
   FIREFLY LUCIFERASE
   SUBUNIT
   CELLS
   GENE
   PHOTOPROTEINS
   EXPRESSION
Аннотация: Major advances in the development and application of the bioluminescent analysis to detect certain biologically active substances are discussed. The main merit of the method lies in its high sensitivity and specificity along with its simplicity and rapid performance. The available methodologies allow for detection of substances of varying nature: Ca2+, ATP, FMN, NAD(P), long-chain aldehydes, ATP- and NAD(P)-dependent enzymes and their substrates, many xenobiotics and antibiotics, and mutagens. The bioluminescence methodologies may be widely applied in clinical laboratory diagnosis.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GITELZON, I.I.; SANDALOVA, T.P.

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13.

NAD(P)H:FMN-Oxidoreductase Functioning Under Macromolecular Crowding: In Vitro Modeling / A. E. Govorun, E. N. Esimbekova, V. A. Kratasyuk // Doklad. Biochem. Biophys. - 2019. - Vol. 486, Is. 1. - P213-215, DOI 10.1134/S160767291903013X . - ISSN 1607-6729
Аннотация: The functioning of NAD(P)H:FMN‑oxidoreductase (Red) from Vibrio fischeri under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin) was studied. The dissociation rate constants and the activation energies of dissociation of Red to the subunits were calculated, and the process of denaturation of Red was analyzed. It is shown that the functioning of Red both under conditions of MMC and in diluted solutions is the same. This result refutes the common belief that the native conformation of enzymes in vivo is stabilized due to MMC as compared to the in vitro conditions. © 2019, Pleiades Publishing, Ltd.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Govorun, A. E.; Esimbekova, E. N.; Kratasyuk, V. A.

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14.

Luminous bacteria as producers of polyhydroxyalkanoates [Text] / A. . Boyandin [et al.] // Macromol. Symp. - 2008. - Vol. 269: 4th European Symposium on Biopolymers (OCT 02-04, 2007, Kusadasi, TURKEY). - P17-22, DOI 10.1002/masy.200850904. - Cited References: 16 . - 6. - ISSN 1022-1360

РУБ Polymer Science
Рубрики:
VIBRIO-HARVEYI
BIOLUMINESCENCE
Кл.слова (ненормированные):
luminous bacteria -- polyhydroxyalkanoates -- polyhydroxybutyrate
Аннотация: The study addresses the ability of luminous bacteria of different taxa (Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio harveyi, Vibrio fischeri) to synthesize polyesters of hydrocarbon acids (polyhydroxyalkanoates, PHAs) as storage macromolecules. The screened strains widely varied in their PHA productivity. Conditions for attaining high polymer yields (including two- and three-component polymers) in batch culture have been determined. The attained polymer yields reached 40-70% of dry cell biomass. The results suggest a conclusion that luminous microorganisms can be considered as producers of multi-component PHAs.

Держатели документа:
[Boyandin, Anatoly
Kalacheva, Galina S.
Medvedeva, Svetlana
Rodicheva, Emma
Volova, Tatiana G.] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
[Volova, Tatiana G.] Siberian Fed Univ, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A...; Kalacheva, G.S.; Medvedeva, S...; Rodicheva, E...; Volova, T.G.

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15.

Luminous bacteria as producers of polyhydroxyalkanoates / A. Boyandin [et al.] // Macromolecular Symposia. - 2008. - Vol. 269, Is. 1. - P17-22, DOI 10.1002/masy.200850904 . - ISSN 1022-1360
Кл.слова (ненормированные):
Luminous bacteria -- Polyhydroxyalkanoates -- Polyhydroxybutyrate -- ABS resins -- Acids -- Bacteriology -- Batch cell culture -- Biological materials -- Biomass -- Biopolymers -- Biotechnology -- Cell culture -- Esters -- Hydrocarbons -- Organic compounds -- Polymers -- Renewable energy resources -- Supramolecular chemistry -- Batch cultures -- Dry cells -- Luminous bacteria -- Micro-organisms -- Photobacterium leiognathi -- Photobacterium phosphoreum -- Polyhydroxyalkanoates -- Polyhydroxybutyrate -- Polymer yields -- Vibrio fischeri -- Bioluminescence
Аннотация: The study addresses the ability of luminous bacteria of different taxa (Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio harveyi, Vibrio fischeri) to synthesize polyesters of hydrocarbon acids (polyhydroxyalkanoates, PHAs) as storage macromolecules. The screened strains widely varied in their PHA productivity. Conditions for attaining high polymer yields (including two- and three-component polymers) in batch culture have been determined. The attained polymer yields reached 40-70% of dry cell biomass. The results suggest a conclusion that luminous microorganisms can be considered as producers of multi-component PHAs. Copyright В© 2008 WILEY-VCH Verlag GmbH & Co. KGaA.

Scopus
Держатели документа:
Institute of Biophysics, SB, RAS, Akademgorodok 50/ 50, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodnyi Av. 79, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A.; Kalacheva, G.S.; Medvedeva, S.; Rodicheva, E.; Volova, T.G.

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16.

Luminous bacteria as potential producers of resorbed polyhydroxyalkanoate polyesters [Text] / A. N. Boyandin [et al.] // Dokl. Biochem. Biophys. - 2007. - Vol. 416, Is. 01.06.2013. - P248-251, DOI 10.1134/S1607672907050067. - Cited References: 15 . - 4. - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VIBRIO-HARVEYI

Держатели документа:
[Boyandin, A. N.
Kalacheva, G. S.
Rodicheva, E. K.
Volova, T. G.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A.N.; Kalacheva, G.S.; Rodicheva, E.K.; Volova, T.G.

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17.

LUMINESCENT PLANKTON BACTERIA FROM THE CORAL REEFS AND LITTORAL WATERS OF THE TROPICAL REGIONS OF THE INDIAN-OCEAN AND THE SOUTH CHINA SEA [Text] / G. A. PRIMAKOVA, A. M. KUZNETSOV // Microbiology. - 1990. - Vol. 59, Is. 5. - P. 630-637. - Cited References: 19 . - ISSN 0026-2617

РУБ Microbiology
Рубрики:
LUMINOUS BACTERIA
   SPECIES COMPOSITION
   MEDITERRANEAN SEA
   ESTUARY
   GULF
   ELAT
Аннотация: Luminescent bacteria were regularly encountered on the coral reefs of both the Indian Ocean and the South China Sea. Their counts in these regions amounted to 10(2) to 10(4) colony-forming units (CFU)/liter, and their proportion of the total numbers of saprophytic bacteria was 0.1-6.0%. Up to 85% of the luminescent bacteria occurred in the sea water in the form of aggregates ranging in size from 3-8-mu-m, to below 200-mu-m. The predominant species amongst the luminescent bacteria of these regions was Vibrio harvevi, comprising [4], with only 8.8% represented by Photobacterium leiognathi.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
PRIMAKOVA, G.A.; KUZNETSOV, A.M.

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18.

Location of lectin exhibiting specificity for N-acetyl-D-galactosamine in cells of the symbiotic marine bacteria Photobacterium phosphoreum [Text] / G. A. Vydryakova, V. S. Bondar // Dokl. Biochem. Biophys. - 2008. - Vol. 420, Is. 1. - P155-157, DOI 10.1134/S1607672908030150. - Cited References: 14 . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VIBRIO-FISCHERI
   EUPRYMNA-SCOLOPES
   LIGHT ORGAN
   COLONIZATION

Держатели документа:
[Vydryakova, G. A.
Bondar, V. S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vydryakova, G.A.; Bondar, V.S.

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19.

Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another / N. S. Rodionova, V. N. Petushkov, P. I. Belobrov // Biophysics. - 1988. - Vol. 33, Is. 3. - P424-430 . - ISSN 0006-3509
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, U.S.S.R. Academy of Sciences, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodionova, N.S.; Petushkov, V.N.; Belobrov, P.I.

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20.

Kinetic analysis of bacterial water-organic media [Text] / I. E. Sukovataya, N. A. Tyulkova // Luminescence. - 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P. 271-273, DOI 10.1002/bio.649.abs. - Cited References: 10 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bacterial luciferase -- organic solvents -- Michaelis constant
Аннотация: The interaction of luciferases from two types of luminous bacteria, Photobacterium leiognathi and Vibrio harveyi, with their substrates [the photorecovered. FMNH2 and long-chain aldehydes-decanal (C-10), dodecanal (C-12) and tetradecanal (C-14)] in water-organic media was analysed using kinetic graphical methods. Moderate concentrations of organic solvents have been demonstrated to activate the bioluminescence, while higher concentrations inhibit it. The interactions of these effectors with luciferases show different types of kinetics, which depend on concentrations of solvents, kinds of enzymes and substrates. The apparent value of the Michaelis constant, K-m for C-14 of both luciferases and for C-10 of luciferase V. harveyi is enhanced with increasing concentration of the organic solvent, but K-m for C-12 and C-10 of luciferase P. leiognathi decreases. Obviously, at the specific binding of aldehydes with luciferases in the first case, hydrophobic interactions are realized, but in second, the electrostatic interactions are realized. The series of changes in parameters of bioluminescence reaction catalysed by different luciferases is obviously determined by their structural peculiarities. Copyright (C) 2001 John Wiley & Sons, Ltd.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sukovataya, I.E.; Tyulkova, N.A.

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