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(19)F NMR study on the biodegradation of fluorophenols by various Rhodococcus species [Text] / V. S. Bondar [et al.] // Biodegradation. - 1998. - Vol. 9: NMR in Environmental Sciences Symposium (OCT 24, 1997, EDE, NETHERLANDS), Is. 6. - P475-486, DOI 10.1023/A:1008391906885. - Cited References: 37 . - ISSN 0923-9820

РУБ Biotechnology & Applied Microbiology
Рубрики:
NUCLEAR-MAGNETIC-RESONANCE
   PSEUDOMONAS-PUTIDA MT-2
   PHENOL HYDROXYLASE
   BACTERIAL-DEGRADATION
   3-OXOADIPATE PATHWAY
   FLUOROBENZOIC ACID
   CONVERSION
   METABOLISM
   CYCLOISOMERASES
   2-CHLORO-CIS,CIS-MUCONATE
Кл.слова (ненормированные):
biodegradation -- fluorophenols -- (19)F NMR -- oxidative defluorination -- Rhodococcus species
Аннотация: Of all NMR observable isotopes (19)F is the one perhaps most convenient for studies on biodegradation of environmental pollutants. The reasons underlying this potential of (19)F NMR are discussed and illustrated on the basis of a study on the biodegradation of fluorophenols by four Rhodococcus strains. The results indicate marked differences between the biodegradation pathways of fluorophenols among the various Rhodococcus species. This holds not only for the level and nature of the fluorinated biodegradation pathway intermediates that accumulate, but also for the regioselectivity of the initial hydroxylation step. Several of the Rhodococcus species contain a phenol hydroxylase that catalyses the oxidative defluorination of ortho-fluorinated di- and trifluorophenols. Furthermore, it is illustrated how the (19)F NMR technique can be used as a tool in the process of identification of an accumulated unknown metabolite, in this case most likely 5-fluoromaleylacetate. Altogether, the (19)F NMR technique proved valid to obtain detailed information on the microbial biodegradation pathways of fluorinated organics, but also to provide information on the specificity of enzymes generally considered unstable and, for this reason, not much studied so far.

Держатели документа:
Agr Univ Wageningen, Dept Biomol Sci, Biochem Lab, NL-6703 HA Wageningen, Netherlands
Russian Acad Sci, Inst Biochem & Physiol Microorganisms, Pushchino 142292, Russia
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondar, V.S.; Boersma, M.G.; Golovlev, E.L.; Vervoort, J...; Van Berkel, WJH; Finkelstein, Z.I.; Solyanikova, I.P.; Golovleva, L.A.; Rietjens, IMCM

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A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL [Text] / V. A. KRATASYUK, V. V. ABAKUMOVA, N. B. KIM // Biochem.-Moscow. - 1994. - Vol. 59, Is. 7. - P. 761-765. - Cited References: 11 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENT
Кл.слова (ненормированные):
BIOLUMINESCENCE -- LUCIFERASE -- NADH, FMN-OXIDOREDUCTASE -- IMMOBILIZATION
Аннотация: A gel model for the functioning of luciferase in cells has been constructed using bacterial NADH:FMN-oxidoreductase and luciferase immobilized in starch gel disks. The characteristics of the immobilized luciferase depend on the duration of drying, the amount and concentration of the gel, the nature of the support used for drying, and the properties of the initial enzyme preparation. Functionally important enzyme groups remain intact in the immobilized preparation, and luciferase retains its high specificity with respect to aldehydes. The gel microenvironment appears to be optimal for luciferase, judging from its high activity and increased stability. Conditions allowing repeated use of the preparation have been found. The approach permits co-immobilization of luciferase with other enzymes and their substrates. The error in bioluminescence measurements using the disks is 5-10%. A procedure for stabilization of the immobilized luciferase during repeated use has been devised.

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

Доп.точки доступа:
KRATASYUK, V.A.; ABAKUMOVA, V.V.; KIM, N.B.

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Active mixing of immobilised enzymatic system in microfluidic chip / K. A. Lukyanenko [et al.] // Micro Nano Lett. - 2017. - Vol. 12, Is. 6. - P377-381, DOI 10.1049/mnl.2016.0646. - Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041). . - ISSN 1750-0443

РУБ Nanoscience & Nanotechnology + Materials Science, Multidisciplinary
Рубрики:
POLY(METHYL METHACRYLATE)
   SURFACE MODIFICATION
   POINT
   DEVICES
   PMMA
Аннотация: Parameters for sample introduction, dried reagents dissolution and mixing with sample for bienzyme system NAD(H):FMN-oxidoreductase and luciferase immobilised in microfluidic chip were successfully determined. Numerical simulations of reaction chamber geometry, flavin mononucleotide (FMN) escape from starch gel and mixing options were conducted to achieve higher sensitivity of bioluminescent reaction. Results of numerical simulations were verified experimentally. The active mixer for dried reagents was made from an electro-mechanical speaker's membrane which was connected to the input of the chip. Such a mixer provided better efficiency than a passive mixing, and it is simple enough for use in point-of-care devices with any systems based on immobilised enzymes in chips.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ITMO Univ, St Petersburg 197101, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, Kirill A.; Belousov, Kirill I.; Denisov, Ivan A.; Yakimov, Anton S.; Esimbekova, Elena N.; Bukatin, Anton S.; Evstrapov, Anatoly A.; Belobrov, Peter I.; Russian Science Foundation [15-19-10041]

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Analytical Enzymatic Reactions in Microfluidic Chips / K. A. Lukyanenko [et al.] // Appl. Biochem. Microbiol. - 2017. - Vol. 53, Is. 7. - P775-780, DOI 10.1134/S0003683817070043. - Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041). . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
BIOAVAILABLE HEAVY-METALS
   DEVICES
   POINT
   LAB
Кл.слова (ненормированные):
bioluminescence -- luciferase -- microfluidics -- microfluidic chip -- enzymatic -- bioassay
Аннотация: A number of approaches have been proposed and tested to transfer enzymatic reactions into the functional elements of microfluidic chips on the example of the bienzyme bioluminescent reaction involving NAD(P)H:FMN-oxidoreductase and luciferase. Measurement of the catalytic activity of these enzymes (under the influence of pollutants) is the basis of enzymatic bioassay of various liquids. It was found that all of the components of the reaction must be placed in the same cell of the chip to improve the reproducibility of the measurements. The use of starch gel as a carrier for immobilization and gelatin as a scaffold in the reactor of the chip enables the preservation of enzyme activity in the course of sealing the chip at room temperature. It is shown that the components of the reaction should be vigorously stirred in a microfluidic chip reactor to improve the efficiency of the analysis. As a result of the studies, a prototype of microfluidic chip based on the enzymatic bioluminescent reaction is proposed. It is characterized by a detection limit of copper sulfate of 3 mu M that corresponds to the sensitivity of traditional lux-biosensors based on living cells. The analysis time is reduced to 1 min, and the analysis can be performed by individuals without special laboratory skills.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
St Petersburg Inst Fine Mech & Opt, St Petersburg 197101, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, K. A.; Denisov, I. A.; Yakimov, A. S.; Esimbekova, E. N.; Belousov, K. I.; Bukatin, A. S.; Kukhtevich, I. V.; Sorokin, V. V.; Evstrapov, A. A.; Belobrov, P. I.; Russian Science Foundation [15-19-10041]

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Antioxidant Activity of Fullerenols. Bioluminescent Monitoring in vitro / A. S. Sachkova [et al.] ; ed.: A. . Turner, A. . Tang // BIOSENSORS 2016 : ELSEVIER SCIENCE BV, 2017. - Vol. 27: 26th Anniversary World Congress on Biosensors (Biosensors) (MAY 25-27, 2016, Gothenburg, SWEDEN). - P230-231. - (Procedia Technology), DOI 10.1016/j.protcy.2017.04.097. - Cited References:2. - The work was supported by the Russian Foundation for Basic Research, Grants No. 15-03-06786 and 15-43-04377-sibir; the state budget to the fundamental research at the Russian Academy of Sciences (project No 01201351504) . -

РУБ Engineering, Biomedical

Кл.слова (ненормированные):
bioluminescence -- enzymatic assay -- toxicity sensor -- antioxidant activity -- fullerenol
Аннотация: Bioluminescence of isolated enzymes is a perspective phenomenon for biosensors development due to simplicity of registration of a physiological parameter - light intensity. Enzyme-based bioluminescent assay is widely used to evaluate a decrease in biochemical toxicities. Also the enzyme-based assay is used for the direct biochemical monitoring of oxidative toxicity. This work considers antioxidant properties of fullerenols, water-soluble polyhydroxylated derivatives of fullerenes and perspective pharmaceutical agents, in solutions of model inorganic and organic toxicants of oxidative type K-3[Fe(CN)(6)] and 1,4-benzoquinone. Two fullerenol preparations were used: C60O2-4(OH)(20-24) and mixture of two types of fullerenols C60O2-4(OH)(20-24)+C70O2-4(OH)(20-24). The enzyme-based assays showed the peculiarities of the detoxification processes: ultralow concentrations of fullerenols were active (ca 10(-17)-10(-5)g/L); no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effects of highly diluted fullerenol solutions were attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. (C) 2017 The Authors. Published by Elsevier Ltd.

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Держатели документа:
Natl Res Tomsk Polytech Univ, Lenin Ave 30, Tomsk 634050, Russia.
SB RAS, Inst Biophys, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny Pr 79, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Vorobeva, A. A.; Kudryasheva, N. S.; Turner, A... \ed.\; Tang, A... \ed.\; Russian Foundation for Basic Research [15-03-06786, 15-43-04377-sibir]; state budget to the fundamental research at the Russian Academy of Sciences [01201351504]

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Applications of luminous bacteria enzymes in toxicology / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescence -- Bioluminescent toxicity enzymatic assay -- Immobilization of enzymes -- Luciferase -- Total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation
Photobiology Laboratory, Russian Academy of Sciences, Siberian Branch, Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

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

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Applications of Luminous Bacteria Enzymes in Toxicology [Text] / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959, DOI 10.2174/1386207318666150917100257. - Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Кл.слова (ненормированные):
Bioluminescence -- bioluminescent toxicity enzymatic assay -- immobilization -- of enzymes -- luciferase -- total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH: FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Esimbekova, Elena N.; Russian Science Foundation [15-19-10041]

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Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide / T. G. Volova, G. S. Kalacheva, O. V. Altukhova // Applied Microbiology and Biotechnology. - 2002. - Vol. 58, Is. 5. - P675-678, DOI 10.1007/s00253-002-0941-8 . - ISSN 0175-7598
Кл.слова (ненормированные):
3 hydroxybutyric acid -- acetoacetyl coenzyme a reductase -- acetyl coenzyme A acyltransferase -- beta hydroxyvalerate -- butyrate dehydrogenase -- carbon monoxide -- electrolyte -- hydrogen -- oxidoreductase -- poly(3 hydroxybutyric acid) -- poly(3 hydroxybutyric acid)synthase -- polyhydroxyalkanoic acid -- polymer -- unclassified drug -- valeric acid -- bacterium -- article -- autotrophy -- bacterial growth -- bacterial strain -- biomass production -- controlled study -- crystallization -- enzyme activity -- molecular weight -- nonhuman -- synthesis -- temperature -- Wautersia eutropha -- Carbon Monoxide -- Culture Media -- Cupriavidus necator -- Fatty Acids -- Lipids -- Polyesters -- Bacteria (microorganisms) -- Negibacteria -- Ralstonia -- Wautersia eutropha
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxy-alkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO (v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (?-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly ?-hydroxybutyrate (more than 99 mol%) with trace amounts of ?-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Br. Russian Academy of Sci., 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Altukhova, O.V.

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Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide [Text] / T. G. Volova, G. S. Kalacheva, O. V. Altukhova // Appl. Microbiol. Biotechnol. - 2002. - Vol. 58, Is. 5. - P. 675-678, DOI 10.1007/s00253-002-0941-8. - Cited References: 35 . - ISSN 0175-7598

РУБ Biotechnology & Applied Microbiology
Рубрики:
PSEUDOMONAS-OLEOVORANS
   ALCALIGENES-EUTROPHUS
   COAL
   CULTIVATION
   METABOLISM
   SUBSTRATE
   CULTURE
   CO2
   H-2
   O-2
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxyalkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (beta-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly beta-hydroxybutyrate (more than 99 mol%) with trace amounts of beta-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Altukhova, O.V.

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10.

Biochemical changes causes lack of bioluminescence in fruiting bodies of Armillaria / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2017. - Vol. 8, Is. 1. - P9-17, DOI 10.5943/mycosphere/8/1/2 . - ISSN 2077-7000
Кл.слова (ненормированные):
Enzymes and substrate of luminescent reaction -- Kinetics of luminescence -- Luminous mycelia -- Nonluminous fruiting bodies of fungus
Аннотация: Mycelium of Armillaria species exhibit bioluminescence in nature and when cultivated on artificial nutrient media. However, fruiting bodies do not emit visible light. The present study investigates biochemical changes which cause this phenomenon. Light emission was studied in experiments with mixtures of cold and hot extracts of the luminous mycelium of Armillaria borealis IBSO 2328 and nonluminous fruiting bodies of this fungus and an unidentified species of the genus (Armillaria sp.). Hot extracts of fruiting bodies of the nonluminous Pholiota squarrosa were used as the substrate analog of the luminescent reaction, as previously this fungus had been found to contain a high amount of this substance. Control experiments showed that cold extracts of A. borealis IBSO 2328 mycelium contained enzymes for the luminescent reaction, which is initiated after addition hot extracts of P. squarrosa fruiting bodies. Parallel experiments with extracts of the fruiting bodies of Armillaria showed that: (i) - cold extracts did not contain enzymes of the luminescent reaction or contain very small amounts of these enzymes and (ii) - hot extracts did not contain substrate of the luminescent reaction. Thus, the reason why fruiting bodies of Armillaria do not emit light is that they do not contain components required for visible luminescence. The study discusses possible causes why the enzymes and substrate of the luminescent reaction are not synthesized in fruiting bodies of Armillaria. © Guizhou Academy of Agricultural Sciences.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Bondar, V. S.

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11.

Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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12.

Characteristics of enclogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fischeri NAD(P)H : FMN-oxidoreductase [Text] / E. V. Vetrova [et al.] // Luminescence. - 2005. - Vol. 20: 11th International Symposium on Luminescence Spectrometry - Detection Techniques in Biomedical and Environmental Analysis (MAY 05-08, 2004, Beijing, JAPAN), Is. 3. - P. 205-209, DOI 10.1002/bio.815. - Cited References: 22 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology
Рубрики:
FLAVODOXIN
   ANISOTROPY
   REDUCTASE
   DYNAMICS
   SYSTEM
Кл.слова (ненормированные):
bacterial bioluminescence -- flavin fluorescence
Аннотация: The bioluminescent bacterial enzyme system NAD(P)H:FMN-oxidoreductase-luciferase has been used as a test system for ecological monitoring. One of the modes to quench bioluminescence is the interaction of xenobiotics with the enzymes, which inhibit their activity. The use of endogenous flavin fluorescence for investigation of the interactions of non-fluorescent compounds with the bacterial luciferase from Photobacterium leiognathi and NAD(P)H:FMN-oxidoreductase from Vibrio fischeri has been proposed. Fluorescence spectroscopy methods have been used to study characteristics of endogenous flavin fluorescence (fluorophore lifetime, the rotational correlation time). The fluorescence anisotropy behaviour of FMN has been analysed and compared to that of the enzyme-bound flavin. The fluorescence characteristics of endogenous flavin of luciferase and NAD(P)H:FMN-oxidoreductase have been shown to be applicable in studying enzymes' interactions with non-fluorescent compounds. Copyright (c) 2005 John Wiley & Sons, Ltd.

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Держатели документа:
RAS, SB, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Wageningen & Res Ctr, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vetrova, E.V.; Kudryasheva, N.S.; Visser, AJWG; van Hoek, A...

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13.

Characteristics of proteins synthesized by hydrogen-oxidizing microorganisms / T. G. Volova, V. A. Barashkov // Applied Biochemistry and Microbiology. - 2010. - Vol. 46, Is. 6. - P574-579, DOI 10.1134/S0003683810060037 . - ISSN 0003-6838
Кл.слова (ненормированные):
Animalia -- Bacteria (microorganisms) -- Cupriavidus necator -- Pseudomonas carboxydohydrogena
Аннотация: The study was conducted to determine the biological value of proteins synthesized by hydrogen-oxidizing microorganisms-the hydrogen bacteria Alcaligenes eutrophus Z1 and Ralstonia eutropha B5786 and the CO-resistant strain of carboxydobacterium Seliberia carboxydohydrogena Z1062. Based on a number of significant parameters characterizing the biological value of a product, the proteins of hydrogen-oxidizing microorganisms have been found to occupy an intermediate position between traditional animal and plant proteins. The high total protein in biomass of these microorganisms, their complete amino acid content, and availability to proteolytic enzymes allow for us to consider these microorganisms as potential protein producers. В© 2010 Pleiades Publishing, Ltd.

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

Доп.точки доступа:
Volova, T.G.; Barashkov, V.A.

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14.

Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

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Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

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15.

Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465. - P1-31, DOI 10.3390/ijms21207465 . - ISSN 1661-6596
Кл.слова (ненормированные):
Analytical systems -- Bioluminescence -- Ca2+-regulated photoprotein -- Coelenterazine -- Luciferase
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Frank, L. A.

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16.

17.

Comparative evaluation of total peroxidase and catalase activities during light emission of luminous fungus Neonothopanus nambi / O. A. Mogilnaya, N. O. Ronzhin, V. S. Bondar // Mycosphere. - 2016. - Vol. 7, Is. 4. - P499-510, DOI 10.5943/mycosphere/7/4/9 . - ISSN 2077-7000
Кл.слова (ненормированные):
Basidiomycetes -- Hydrogen peroxide -- Luminescence -- Stress
Аннотация: Submerged cultivation of luminous fungus Neonothopanus nambi under orbital stirring causes formation of pellets with smooth or rough surfaces. The experiments showed that luminescence of the pellets washed in water increased considerably. Previous studies suggested possible participation of peroxidases in the light emitting reaction. In this study, oxidative azo coupling reaction accompanied by formation of chromogen was used to evaluate peroxidase activity in vivo, in brightly luminescent pellets and in pellets with low luminescence intensity (dim ones). Staining of the brightly luminescent pellets took a few minutes, and their staining intensity was several times higher than that of the dim pellets. From the results of in vivo experiments it was concluded that the bright pellets differed from the dim ones in the production of hydrogen peroxide, or, possibly, other peroxides. Measurements of total peroxidase and catalase activities in pellet extracts also showed an increase in enzyme activities along with an increase in luminescence intensity of native pellets. However, results of the in vitro experiments do not definitively suggest a direct relationship between luminescence and activity of these enzymes. We assume that luminescence of this fungal species may be an additional way to neutralize peroxide compounds under stress. © Guizhou Academy of Agricultural Sciences.

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Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Bondar, V. S.

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18.

Comparative study of temperature effects on bacterial luciferases [Text] / N. A. Tyulkova, T. P. Sandalova // Biochem.-Moscow. - 1996. - Vol. 61, Is. 2. - P. 205-214. - Cited References: 23 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENCE
Кл.слова (ненормированные):
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.

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

Доп.точки доступа:
Tyulkova, N.A.; Sandalova, T.P.

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19.

Creation of Bifunctional Indicating Complex Based on Nanodiamonds and Extracellular Oxidases of Luminous Fungus Neonothopanus nambi / O. A. Mogilnaya [et al.] // Dokl. Biochem. Biophys. - 2018. - Vol. 480, Is. 1. - P135-138, DOI 10.1134/S160767291803002X. - Cited References:13 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PHANEROCHAETE-CHRYSOSPORIUM
NANOPARTICLES
Аннотация: A bifunctional indicating complex was created by immobilization of extracellular oxidases (glucose oxidase and peroxidases) of luminous fungus Neonothopanus nambi onto modified nanodiamonds (MNDs) synthesized by detonation. It was found that the enzymes firmly adsorb onto MND particles and exhibit their catalytic activity. Model in vitro experiments showed that the created MND-enzymes complex is suitable for repeated use for analyte (glucose and phenol) testing and retains its activity after storage at 4 degrees C in deionized water for 1 month. The data obtained offer the prospects for developing a new class of reusable multifunctional indicating and diagnostic test systems on the basis of MNDs and higher fungal enzymes for medical and ecological analytics.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Artemenko, K. S.; Bondar, V. S.

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20.

Degradation of P(3HB) and P(3HB-co-3HV) in biological media / E. I. Shishatskaya [et al.] // Journal of Biomaterials Science, Polymer Edition. - 2005. - Vol. 16, Is. 5. - P643-657, DOI 10.1163/1568562053783678 . - ISSN 0920-5063
Кл.слова (ненормированные):
Degradation rate -- Fiber properties -- Morphology -- Poly(hydroxybutyrate-co-hydroxyvalerate) (P(3HB-co-3HV)) -- Polyhydroxyalkanoates(PHAs) -- Polyhydroxybutyrate (P(3HB)) -- Copolymers -- Degradation -- Differential scanning calorimetry -- Enzymes -- Morphology -- Scanning electron microscopy -- Tensile strength -- Tissue -- Transmission electron microscopy -- Degradation rate -- Fiber properties -- Polyhydroxyalkanoates (PHAs) -- Polyhydroxybutyrate (P(3HB)) -- Biopolymers -- buffer -- copolymer -- poly(3 hydroxybutyric acid) -- polyhydroxybutyrate hydroxyvalerate copolymer -- unclassified drug -- animal experiment -- animal model -- animal tissue -- article -- biodegradation -- controlled study -- crystal structure -- fiber -- giant cell -- in vitro study -- in vivo study -- macrophage -- morphology -- nonhuman -- pH -- priority journal -- rat -- structure analysis -- tensile strength -- tissue water -- weight reduction -- Animals -- Biodegradation, Environmental -- Buffers -- Humans -- Hydrogen-Ion Concentration -- Hydroxybutyrates -- Macrophages -- Microscopy, Electron, Scanning -- Microscopy, Electron, Transmission -- Muscle, Skeletal -- Polyesters -- Rats -- Rats, Wistar
Аннотация: The biodegradability of oriented fibers made of polyhydroxybutyrate (P(3HB)) and its co-polymer with ?-hydroxyvalerate (P(3HB-co-3HV)) was investigated in buffer solutions and in biological media in vitro and in vivo. The fibers of both polymer types demonstrated resistance to hydrolytic degradation in buffer solutions at 38В°C and pH from 4.5 to 7.0 (for up to 180 days). It has been found that the biodegradation of the fibers in vitro in blood and serum and in vivo is accompanied by weight losses and minor changes in the microstructure with no significant losses in the tensile strength over a long time (up to 180 days). The biodegradation rate of the less crystalline co-polymer P(3HB-co-3HV) fibers was 1.4-2.0-times higher than that of the homopolymer P(3HB). It has also been shown that the degradation of the fibers in vivo is influenced both by tissue fluid enzymes and cells (macrophages and foreign-body giant cells). The fibers were eroded on the surface only with no gross defects and no dramatic effects on their mechanical performance. В© VSP 2005.

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Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 600326, Russian Federation
Department of Cardiac Surgery, University of Glasgow, Royal Infirmary, 10 Alexandra Parade, Glasgow G3, United Kingdom : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shishatskaya, E.I.; Volova, T.G.; Gordeev, S.A.; Puzyr, A.P.

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