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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Бояндин А.Н., Калачева Г.С., Родичева Э.К., Волова Т.Г.
Заглавие : Синтез резервных полигидроксиалканоатов светящимися бактериями : научное издание
Место публикации : Микробиология. - 2008. - Т. 77, N 3. - С. 364-369. - ISSN 0026-3656
ГРНТИ : 34.27.17
Предметные 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Boyandin A., Kalacheva G.S., Medvedeva S., Rodicheva E., Volova T.G.
Заглавие : Luminous bacteria as producers of polyhydroxyalkanoates
Место публикации : Macromolecular Symposia. - 2008. - Vol. 269, Is. 1. - С. 17-22. - ISSN 10221360 (ISSN) , DOI 10.1002/masy.200850904
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Boyandin A.N., Kalacheva G.S., Rodicheva E.K., Volova T.G.
Заглавие : Synthesis of reserve polyhydroxyalkanoates by luminescent bacteria
Место публикации : Microbiology. - 2008. - Vol. 77, Is. 3. - С. 318-323. - ISSN 00262617 (ISSN) , DOI 10.1134/S0026261708030119
Ключевые слова (''Своб.индексиров.''): 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.
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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) : 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) : 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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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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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.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Boyandin A..., Kalacheva G.S., Medvedeva S..., Rodicheva E..., Volova T.G.
Заглавие : Luminous bacteria as producers of polyhydroxyalkanoates
Место публикации : Macromol. Symp.: WILEY-V C H VERLAG GMBH, 2008. - Vol. 269: 4th European Symposium on Biopolymers (OCT 02-04, 2007, Kusadasi, TURKEY). - С. 17-22. - 6. - ISSN 1022-1360, DOI 10.1002/masy.200850904
Примечания : Cited References: 16
Предметные рубрики: VIBRIO-HARVEYI
BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Boyandin A.N., Kalacheva G.S., Rodicheva E.K., Volova T.G.
Заглавие : Luminous bacteria as potential producers of resorbed polyhydroxyalkanoate polyesters
Место публикации : Dokl. Biochem. Biophys.: SPRINGER, 2007. - Vol. 416, Is. 01.06.2013. - С. 248-251. - 4. - ISSN 1607-6729, DOI 10.1134/S1607672907050067
Примечания : Cited References: 15
Предметные рубрики: VIBRIO-HARVEYI
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Titushin M.S., Feng Y.G., Lee J..., Vysotski E.S., Liu Z.J.
Заглавие : Protein-protein complexation in bioluminescence
Колич.характеристики :16 с
Место публикации : Protein Cell: HIGHER EDUCATION PRESS, 2011. - Vol. 2, Is. 12. - С. 957-972. - ISSN 1674-800X, DOI 10.1007/s13238-011-1118-y
Примечания : 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).
Предметные 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
Ключевые слова (''Своб.индексиров.''): 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.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Visser N.V., van Hoek A..., Skakun V.V., Vysotski E.S., Lee J..., Visser AJWG
Заглавие : Green-Fluorescent Protein from the Bioluminescent Jellyfish Clytia gregaria Is an Obligate Dimer and Does Not Form a Stable Complex with the Ca2+-Discharged Photoprotein Clytin
Колич.характеристики :10 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2011. - Vol. 50, Is. 20. - С. 4232-4241. - ISSN 0006-2960, DOI 10.1021/bi101671p
Примечания : Cited References: 50. - This work was supported by NATO Collaborative Linkage Grant 979229, Grants SB RAS No. 2 and RFBR 08-04-92209, 09-04-12022, and 09-04-00172, the MCB program of the Russian Academy of Sciences, and Bayer AG.
Предметные рубрики: VIBRIO-FISCHERI Y1
ENERGY-TRANSFER
CORRELATION SPECTROSCOPY
BACTERIAL LUCIFERASE
REFRACTIVE-INDEX
PHOTOBACTERIUM-LEIOGNATHI
POLARIZED FLUORESCENCE
EXCITATION TRANSFER
RECOMBINANT OBELIN
LUMAZINE PROTEIN
Аннотация: Green-fluorescent protein (GFP) is the origin of the green bioluminescence color exhibited by several marine hydrozoans and anthozoans. The mechanism is believed to be Forster resonance energy transfer (FRET) within a luciferase GFP or photoprotein-GFP complex. As the effect is found in vitro at micromolar concentrations, for FRET to occur this complex must have an affinity in the micromolar range. We present here a fluorescence dynamics investigation of the recombinant bioluminescence proteins from the jellyfish Clytia gregaria, the photoprotein clytin in its Ca2+-discharged form that is highly fluorescent (lambda(max) = 506 nm) and its GFP (cgreGFP; lambda(max) = 500 nm). Ca2+-discharged clytin shows a predominant fluorescence lifetime of 5.7 ns, which is assigned to the final emitting state of the bioluminescence reaction product, coelenteramide anion, and a fluorescence anisotropy decay or rotational correlation time of 12 ns (20 degrees C), consistent with tight binding and rotation with the whole protein. A 34 ns correlation time combined with a translational diffusion constant and molecular brightness from fluorescence fluctuation spectroscopy all confirm that cgreGFP is an obligate dimer down to nanomolar concentrations. Within the dimer, the two chromophores have a coupled excited-state transition yielding fluorescence depolarization via FRET with a transfer correlation time of 0.5 ns. The 34 ns time of cgreGFP showed no change upon addition of a 1000-fold excess of Ca2+-discharged clytin, indicating no stable complexation below 0.2 mM. It is proposed that any bioluminescence FRET complex with micromolar affinity must be one formed transiently by the cgreGFP dimer with a short-lived (millisecond) intermediate in the clytin reaction pathway.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vydryakova G.A., Bondar V.S.
Заглавие : Location of lectin exhibiting specificity for N-acetyl-D-galactosamine in cells of the symbiotic marine bacteria Photobacterium phosphoreum
Колич.характеристики :3 с
Место публикации : Dokl. Biochem. Biophys.: SPRINGER, 2008. - Vol. 420, Is. 1. - С. 155-157. - ISSN 1607-6729, DOI 10.1134/S1607672908030150
Примечания : Cited References: 14
Предметные рубрики: VIBRIO-FISCHERI
EUPRYMNA-SCOLOPES
LIGHT ORGAN
COLONIZATION
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14.

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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15.

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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16.

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.
Scopus
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17.

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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18.

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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19.

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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20.

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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