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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : GUREVICH V.B., SVETLAKOV A.V., POPOVA L.Y., SHENDEROV A.N.
Заглавие : GLUTAMATE SYNTHESIS CONTROL IN VIBRIO-HARVEYI
Колич.характеристики :3 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1986. - Vol. 55, Is. 1. - P66-68. - ISSN 0026-2617
Примечания : Cited References: 10
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodionova N.S., Petushkov V.N., Belobrov P.I.
Заглавие : Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another
Место публикации : Biophysics. - 1988. - Vol. 33, Is. 3. - С. 424-430. - ISSN 00063509 (ISSN)
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Гительзон И.И., Воробьева Т.И.
Заглавие : Светящиеся бактерии, ассоциированные с бентосными организмами : научное издание
Место публикации : Микробиология. - 1988. - Т. 57, N 5. - С. 847-852
ГРНТИ : 34.27.53
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : PRIMAKOVA G.A., KUZNETSOV A.M.
Заглавие : LUMINESCENT PLANKTON BACTERIA FROM THE CORAL REEFS AND LITTORAL WATERS OF THE TROPICAL REGIONS OF THE INDIAN-OCEAN AND THE SOUTH CHINA SEA
Колич.характеристики :8 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1990. - Vol. 59, Is. 5. - P630-637. - ISSN 0026-2617
Примечания : Cited References: 19
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarrionov B.A., Blinov V.M., Douchenko A.P., Protopopova M.V., Karginov V.A., Mertvetsov N.P., Gitelson J.I.
Заглавие : Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes
Место публикации : Gene. - 1990. - Vol. 86, Is. 1. - С. 89-94. - ISSN 03781119 (ISSN)
Ключевые слова (''Своб.индексиров.''): bioluminescence--expression in e. coli--luciferase--molecular evolution--nucleotide sequence--protein alignment--recombinant dna--luciferase--amino acid sequence--article--bioluminescence--fungus--gene structure--genetic engineering--heredity--nonhuman--nucleotide sequence--priority journal--vibrionaceae--acyltransferases--amino acid sequence--bacterial proteins--base sequence--cloning, molecular--dna, bacterial--genes, structural, bacterial--luciferase--luminescence--molecular sequence data--operon--photobacterium--restriction mapping--escherichia coli--fungi--photobacterium leiognathi--vibrio harveyi--vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : GITELZON I.I., SANDALOVA T.P.
Заглавие : PROSPECTS FOR APPLICATION OF BIOLUMINESCENCE METHOD IN MEDICINE
Колич.характеристики :5 с
Место публикации : VESTNIK AKADEMII MEDITSINSKIKH NAUK SSSR: IZD VO MEDITSINA, 1990. - Is. 9. - С. 31-35. - ISSN 0002-3027
Примечания : Cited References: 41
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stom D.I., Geel T.A., Balayan A.E., Shachova G.I., Kuznetsov A.M., Medvedeva S.E.
Заглавие : Bioluminescent method in studying the complex effect of sewage components
Место публикации : Archives of Environmental Contamination and Toxicology. - 1992. - Vol. 22, Is. 2. - С. 203-208. - ISSN 00904341 (ISSN)
Ключевые слова (''Своб.индексиров.''): heavy metal--phenol derivative--quinone derivative--article--bacterium--bioluminescence--cell membrane--nonhuman--priority journal--sludge--ultrastructure--benzoquinones--catechin--hydroquinones--luminescent measurements--metals--phenol--phenols--photobacterium--sewage--vibrio--water pollutants, chemical--bacteria (microorganisms)
Аннотация: The inhibition of bacterial luminescence has been used in testing industrial enterprises sewage. The toxicity of the sewage is less than the total toxicity of separate components due to neutralization of quinone products of polyphenol oxidation in the reactions with the other phenol components of sewage. Toxicity increase is due to their influence on the cell membrane. Studies of cell ultrastructure confirm this fact. The studied mechanism of the complex effect allowed a more accurate forecast of the ecological situation during the discharge of phenol compounds and metals. It also showed the necessity of taking into account the complex effect of sewage components on contaminant discharge into water reservoirs.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : SANDALOVA T.P., TYULKOVA N.A.
Заглавие : INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE
Колич.характеристики :7 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 6. - P552-558. - ISSN 0006-2979
Примечания : Cited References: 21
Предметные рубрики: AMINO-ACID SEQUENCE
NUCLEOTIDE-SEQUENCE
REACTIVE SULFHYDRYL
PHOTOBACTERIUM-LEIOGNATHI
VIBRIO-HARVEYI
BIOLUMINESCENCE
SUBUNIT
REGION
GENE
Ключевые слова (''Своб.индексиров.''): luciferase--n-ethylmaleimide
Аннотация: The kinetics of inactivation of luciferases from four species of luminescent bacteria by the thiol reagent N-ethylmaleimide were investigated The dependencies of inactivation on ionic strength differed among the enzymes. Increasing the molarity of the buffer increased the rate of inactivation of all luciferases except that of Vibrio harveyi. Modification of Photobacterium phosphoreum luciferase decreased the maximal intensity of bioluminescence, whereas modification of Photobacterium leiognathi and Vibrio fischeri luciferases in high ionic strength buffers decreased the maximal intensity of bioluminescence and changed the luminescence decay rate constant. High ionic strength apparently alters the conformational states of the luciferases.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Rodicheva E.K., Trubachev I.N., Medvedeva S.E., Egorova O.I. U - Shitova LYu
Заглавие : Growth and luminescence of luminous bacteria promoted by agents of microbial origin.
Место публикации : Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - С. 293-299. - ISSN 08843996 (ISSN)
Ключевые слова (''Своб.индексиров.''): amino acid--carbohydrate--folic acid--luciferase--nitrogen--riboflavin--article--biosynthesis--culture medium--electron microscopy--growth, development and aging--kinetics--luminescence--metabolism--photobacterium--physiology--time--ultrastructure--vibrio--amino acids--carbohydrates--culture media--folic acid--kinetics--luciferase--luminescence--microscopy, electron--nitrogen--photobacterium--riboflavin--time factors--vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J.
Заглавие : The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein
Место публикации : Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - С. 774-779. - ISSN 0006291X (ISSN) , DOI 10.1006/bbrc.1995.1880
Ключевые слова (''Своб.индексиров.''): 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.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tyulkova N.A., Sandalova T.P.
Заглавие : Comparative study of temperature effects on bacterial luciferases
Колич.характеристики :10 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1996. - Vol. 61, Is. 2. - P205-214. - ISSN 0006-2979
Примечания : Cited References: 23
Предметные рубрики: BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): bacterial luciferase--temperature--activation energy
Аннотация: Effects of temperature on bioluminescent patterns of luciferases from luminescent bacteria Vibrio harveyi, Vibrio fischeri, Photobacterium leiognathi, and Photobacterium phosphoreum were studied. The highest luminescence level was observed at 15-25 degrees C for the luciferase from P. phosphoreum, at 20-30 degrees C for the V. fischeri and P. leiognathi enzymes, and at 30-37 degrees C for the enzyme from V. harveyi. All the luciferases were significantly stabilized at increased salt concentrations, at low pH values, or in the presence of dithiothreitol (DTT) and EDTA. The addition of DTT and EDTA affected the reversible stage of enzyme inactivation, while salts reduced the rate of the irreversible stage. A peak corresponding to aggregated protein was detected by gel chromatography of irreversibly inactivated luciferase. Activation energies were calculated for each luciferase in bioluminescent reactions with decanal, dodecanal, tetradecanal, and without aldehydes. The activation energy of the reaction with tetradecanal was much lower than those with the other aldehydes. The temperature dependence of the lifetime of the long-lived reaction intermediate showed that in the 10-30 degrees C interval all the luciferases, except for the enzyme from V. harveyi, have only one active form.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M., Gibson B.G., Lee J.
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive
Место публикации : Biochemistry. - 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 00062960 (ISSN) , DOI 10.1021/bi9608931
Ключевые слова (''Своб.индексиров.''): luciferase--anisotropy--antenna--article--bioluminescence--complex formation--energy transfer--enzyme active site--enzyme kinetics--nonhuman--priority journal--protein protein interaction--spectroscopy--vibrionaceae--bacterial proteins--carrier proteins--cloning, molecular--dithionite--flavin mononucleotide--kinetics--luciferases--luminescent measurements--luminescent proteins--models, structural--photobacterium--protein binding--protein conformation--recombinant proteins--spectrophotometry--vibrio--bacteria (microorganisms)--photobacterium--photobacterium leiognathi--vibrio fischeri--vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J...
Заглавие : Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1
Колич.характеристики :6 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 25. - С. 8413-8418. - ISSN 0006-2960, DOI 10.1021/bi952691v
Примечания : Cited References: 24
Предметные рубрики: LUMAZINE PROTEIN
LUMINOUS BACTERIUM
STRAIN Y-1
BIOLUMINESCENCE
EMISSION
PURIFICATION
TRANSIENT
LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M..., Gibson B.G., Lee J...
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive
Колич.характеристики :8 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 0006-2960, DOI 10.1021/bi9608931
Примечания : Cited References: 41
Предметные рубрики: BACTERIAL LUCIFERASE
LUMAZINE PROTEIN
FLAVIN INTERMEDIATE
ANGSTROM RESOLUTION
RIBOFLAVIN PROTEIN
PURIFICATION
MECHANISM
EMISSION
ALDEHYDE
INHIBITION
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects call be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, when the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on-off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme, These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found or the protein-protein interaction in the absence of the aliphatic component.
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Lee J.
Заглавие : Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1
Место публикации : European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - С. 790-796. - ISSN 00142956 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Medvedeva S.E.
Заглавие : Transfer of xenobiotics through cell membranes of luminous bacteria
Место публикации : Luminescence. - 1999. - Vol. 14, Is. 5. - С. 267-270. - ISSN 15227235 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petrushkov V.N., Gibson B.G., Visser AJWG, Lee J...
Заглавие : Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria
Колич.характеристики :17 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - P164-180. - ISSN 0076-6879
Примечания : Cited References: 18
Предметные рубрики: YELLOW FLUORESCENT PROTEIN
FISCHERI STRAIN Y-1
AMINO-ACID-SEQUENCE
VIBRIO-FISCHERI
PHOTOBACTERIUM-LEIOGNATHI
RIBOFLAVIN PROTEIN
LUMINOUS BACTERIUM
LUMAZINE PROTEIN
FMN
Y1
WOS
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sukovataya I.E., Tyulkova N.A.
Заглавие : Kinetic analysis of bacterial water-organic media
Колич.характеристики :3 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P271-273. - ISSN 1522-7235, DOI 10.1002/bio.649.abs
Примечания : Cited References: 10
Ключевые слова (''Своб.индексиров.''): 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.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Van Stokkum I.H.M., Gobets B., Van Mourik F., Lee J., Van Grondelle R., Visser A.J.W.G.
Заглавие : Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
Место публикации : Journal of Physical Chemistry B. - 2003. - Vol. 107, Is. 39. - С. 10934-10939. - ISSN 15206106 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., van Stokkum IHM, Gobets B..., van Mourik F..., Lee J..., van Grondelle R..., Visser AJWG
Заглавие : Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
Колич.характеристики :6 с
Место публикации : J. Phys. Chem. B: AMER CHEMICAL SOC, 2003. - Vol. 107, Is. 39. - P10934-10939. - ISSN 1520-6106, DOI 10.1021/jp034266e
Примечания : Cited References: 52
Предметные 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.
WOS
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