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Accumulation of 242Pu by a macrophyte of the Yenisei River (Elodea canadensis) in laboratory experiments / A. Bolsunovsky [et al.] // Chemosphere. - 2009. - Vol. 75, Is. 3. - P284-288, DOI 10.1016/j.chemosphere.2008.12.036 . - ISSN 0045-6535
Кл.слова (ненормированные):
242Pu -- Accumulation -- Laboratory experiments -- Sequential extraction technique -- Submerged plant Elodea canadensis -- Yenisei River -- sup242/supPu -- Accumulation -- Laboratory experiments -- Sequential extraction technique -- Submerged plant Elodea canadensis -- Yenisei River -- Biological materials -- Biomass -- Chemical plants -- Experiments -- Positive ions -- Rivers -- Plutonium -- concentration (composition) -- experimental study -- laboratory method -- macrophyte -- plutonium isotope -- river water -- submerged vegetation -- Eurasia -- Russian Federation -- Yenisei River -- plutonium -- article -- biomass -- chemistry -- Hydrocharitaceae -- physiology -- plant -- radiation monitoring -- river -- time -- water pollutant -- Biomass -- Hydrocharitaceae -- Plant Shoots -- Plutonium -- Radiation Monitoring -- Rivers -- Time Factors -- Water Pollutants, Radioactive
Аннотация: The study addresses 242Pu accumulation by Elodea canadensis, one of the abundant species of submerged plants in the Yenisei River. 242Pu in water samples of the "Elodea - Yenisei River water" model system and in the biomass fractions was determined ?-spectrometrically, following radiochemical recovery of 242Pu using 236Pu - a chemical yield tracer. The experiments on accumulation of 242Pu by Elodea biomass showed that the activity concentration of 242Pu can reach 21 В± 2 Bq/g dry wt, with the concentration factor for 242Pu 13100 В± 2100 L/kg dry wt. Results of chemical fractionation proved that during the first few hours of the experiment 242Pu contained in Elodea was mainly concentrated in the exchangeable and the adsorbed fractions of biomass (about 100%). As Elodea biomass accumulated 242Pu, the absolute amount of 242Pu in the exchangeable and the adsorbed fractions remained almost unchanged, although the portion of 242Pu tightly bound to biomass increased. At the end of the experiment, on day 7, 242Pu tightly bound to biomass (fractions of organics and mineral residue) constituted 43-63% (in different experiments) of the total 242Pu in the biomass. В© 2008 Elsevier Ltd. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, the Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Institute of Geology and Mineralogy, Siberian Branch, the Russian Academy of Sciences, Novosibirsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bolsunovsky, A.; Bondareva, L.; Sukhorukov, F.; Melgunov, M.

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Effect of NaCl concentration on productivity and mineral composition of Salicornia europaea as a potential crop for utilization NaCl in LSS / S. A. Ushakova [et al.] // Advances in Space Research. - 2005. - Vol. 36, Is. 7. - P1349-1353, DOI 10.1016/j.asr.2004.09.017 . - ISSN 0273-1177
Кл.слова (ненормированные):
Life support system -- NaCl -- Salicornia europaea -- Space biology -- Calcium -- Concentration (process) -- Minerals -- Photosynthesis -- Plants (botany) -- Salinity measurement -- Sodium chloride -- Vegetation -- Life support systems -- Liquid wastes -- NaCl -- Salicornea europea -- Space biology -- Space research
Аннотация: The accumulation of solid and liquid wastes in manmade ecosystems presents a problem that has not been efficiently solved yet. Urine, containing NaCl, are part of these products. This is an obstacle to the creation of biological systems with a largely closed material cycling, because the amount of solid and liquid wastes in them must be reduced to a minimum. A possible solution to the problem is to select plant species capable of utilizing sufficiently high concentrations of NaCl, edible for humans, and featuring high productivity. Until recently, the life support systems have included the higher plants that were either sensitive to salinization (wheat, many of the legumes, carrot, potato, maize) or relatively salt-resistant (barley, sugar beet, spinach). Salicomia europaea, whose above-ground part is fully edible for humans, is one of the most promising candidates to be included in life support systems. It is reported in the literature that this plant is capable of accumulating up to 50% NaCl (dry basis). Besides, excessive accumulation of sodium ions should bring forth a decrease in the uptake of potassium ions and other biogenic elements. The aim of this work is to study the feasibility of using S. europaea plants in growth chambers to involve NaCl into material cycling. Plants were grown in vegetation chambers at the irradiance of 100 or 150 W/m2 PAR (photosynthetically active radiation) and the air temperature 24 В°C, by two methods. The first method was to grow the plants on substrate - peat. The peat was supplemented with either 3% NaCl (Variant 1) or 6% NaCl (Variant 2) of the oven-dry mass of the peat. The second method was to grow the plants in water culture, using the solution with a full complement of nutrients, which contained 0.0005% of NaCl, 1% or 2%. The study showed that the addition of NaCl to the substrate or to the solution resulted in the formation of more succulent plants, which considerably increased their biomass. The amount of NaCl uptake was the highest in the plants grown in water culture, 2.6 g per plant. As the sodium uptake increased, the consumption of potassium and the sum of the reduced N forms decreased twofold. The uptake of calcium and magnesium by plants decreased as the NaCl concentration increased; the smallest amounts were taken up by S. europaea grown in water culture. Salinity had practically no effect on the uptake of phosphorus and sulfur. Thus, S. europaea is a promising candidate to be included in life support systems; of special interest is further research on growing these plants in water culture. В© 2005 COSPAR. Published by Elsevier Ltd. All rights reserved.

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

Доп.точки доступа:
Ushakova, S.A.; Kovaleva, N.P.; Gribovskaya, I.V.; Dolgushev, V.A.; Tikhomirova, N.A.

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Luminescence of Ca(2+)-activated photoprotein obelin initiated by NaOCl and MnCl2. / E. S. Vysotski [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P301-305 . - ISSN 0884-3996
Кл.слова (ненормированные):
calcium -- chloride -- hypochlorite sodium -- manganese chloride -- manganese derivative -- obelin -- photoprotein -- article -- chemistry -- drug effect -- kinetics -- luminescence -- metabolism -- Calcium -- Chlorides -- Kinetics -- Luminescence -- Luminescent Proteins -- Manganese Compounds -- Sodium Hypochlorite
Аннотация: The luminescence of obelin is initiated by NaOCl in a reaction mixture containing no calcium. The addition of Mn2+ enhances the light emission > 300-fold. Sodium azide and histidine, as singlet oxygen quenchers, inhibit NaOCl-activated obelin luminescence in the presence or absence of Mn2+. This suggests that the addition of NaOCl to the mixture causes singlet oxygen formation (stimulated by Mn2+ ions), and singlet oxygen initiates the light-emitting reaction.

Scopus
Держатели документа:
Laboratory of Photobiology, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Trofimov, K.P.; Bondar', V.S.; Gitelson, J.I.

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Affine magnetic sorbents supported on coal ash microspheres for recombinant protein isolation / L. A. Frank [et al.] // Applied Biochemistry and Microbiology. - 2009. - Vol. 45, Is. 2. - P215-220, DOI 10.1134/S0003683809020173 . - ISSN 0003-6838
Кл.слова (ненормированные):
Clytia gregaria -- Obelia longissima
Аннотация: The results of the development and utilization of an affine magnetic sorbent with Ni2+ ions immobilized on coal ash microspheres are reported. The applicability of the material in the isolation of Histag proteins is demonstrated by examples of the recombinant green fluorescent protein from Clytia gregaria and the Ca2+ regulated photoprotein obelin from Obelia longissima. The specific sorption capacity of the sorbent was 2-7 mg/cm3 for medium-size proteins (20-30 kDa). The particles are suitable for chromatography with the presence of chaotropic agents and EDTA. They are easy to manipulate as isolation of a target protein takes 30-35 min. On the one hand, the elevated affinity of the sorbent to proteins rich in native histidines may result in a high degree of irreversible sorption; on the other hand, it allows isolation of such proteins without the introduction of artificial polyhistidine fragments. В© 2009 Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Institute of Chemistry and Chemical Technology, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660049, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Vereshchagina, T.A.; Fomenko, E.V.; Anshits, A.G.; Gitelson, I.I.

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MN2+-ACTIVATED LUMINESCENCE OF THE PHOTOPROTEIN OBELIN [Text] / E. S. VYSOTSKI [et al.] // Arch. Biochem. Biophys. - 1995. - Vol. 316, Is. 1. - P92-99, DOI 10.1006/abbi.1995.1014. - Cited References: 38 . - 8. - ISSN 0003-9861

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   CA-2+-ACTIVATED PHOTOPROTEIN
   MESSENGER-RNA
   BEROE-OVATA
   AEQUORIN
   PURIFICATION
   PROTEIN
   CDNA
   EXTRACTION
Аннотация: The light emission of obelin may be initiated by Mn2+ under alkaline conditions. The luminescence takes place in a pH range from 7 to 12 with a sharp optimum at 11.75. The first-order rate constant for Mn2+-activated luminescence decay is more than 9 s(-1), while that for Ca2+-activated luminescence decay is only 6.9 s(-1). The Mn2+ concentration-effect curve for obelin determined with simple dilutions of manganese salt is a sigmoid curve, The slope of the curve is moderately dependent on the pH and was not more than 1 within the pH range tested. The maximal light emission, which is initiated by 3.6 X 10(-5) M Mn2+ at pH 11.75 was about 10% of the maximal Ca2+-activated luminescence. Mg2+ ions inhibit the Mn2+-activated luminescence of obelin. The addition of OH. and O-2(-) scavengers did not influence the Mn2+-activated luminescence, but when singlet oxygen quenchers were added, the Mn2+-dependent light emission was inhibited. This suggests that the O-1(2) might be formed and itself be responsible for chromophore oxidation attended with light emission. NEM and Na2S2O4 inhibit the Mn2+-initiated light emission of obelin completely, showing that endogenous hydroperoxide and SH-group(s) of the photoprotein are essential for both Ca2+-activated and Mn2+-activated light emission of obelin. (C) 1995 Academic Press, Inc.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
VYSOTSKI, E.S.; TROFIMOV, C.P.; BONDAR, V.S.; FRANK, L.A.; MARKOVA, S.V.; ILLARIONOV, B.A.

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THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN AS AN INDICATOR OF CALCIUM-TRANSPORT IN PROTEOLIPOSOMES CONTAINING MEMBRANES OF THE T-SYSTEM OF SKELETAL-MUSCLES [Text] / V. S. BONDAR [et al.] // Biochem.-Moscow. - 1991. - Vol. 56, Is. 5. - P546-550. - Cited References: 12 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CHANNEL
   CA-2+
   MODULATION
   BINDING
Кл.слова (ненормированные):
CA2+-TRANSPORT -- CA2+-ACTIVATED PHOTOPROTEIN OBELIN -- T-SYSTEM -- 1,4-DIHYDROPYRIDINES -- LIPOSOMES
Аннотация: Data are presented on the Ca2+-activated photoprotein obelin as an indicator of calcium transport in proteoliposomes. Proteoliposomes formed from lecithin and membranes of the T-system of rabbit skeletal muscles were found to exhibit permeability to calcium ions activated by 10(-5) M BAU K-8644; 5.10(-5) M nitrendipine inhibits the action of BAU K-8644. Liposomes did not exhibit sensitivity to the investigated agents. The Ca2+-activated photoprotein obelin is a promising tool for studying fast calcium currents.

Держатели документа:
ACAD SCI USSR,INST BIOPHYS,KRASNOYARSK,USSR
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; VYSOTSKII, E.S.; ROZHMANOVA, O.M.; VORONINA, S.G.

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A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN [Text] / L. Y. Antipina [et al.] // J. Struct. Chem. - 2011. - Vol. 52, Is. 5. - P870-875. - Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213). . - ISSN 0022-4766

РУБ Chemistry, Inorganic & Nuclear + Chemistry, Physical
Рубрики:
CALCIUM-DISCHARGED OBELIN
   SEMIEMPIRICAL METHODS
   1.7 ANGSTROM
   OPTIMIZATION
   PARAMETERS
   MECHANISM
   FLUORESCENCE
   ELEMENTS
   PROTEIN
   EMITTER
Кл.слова (ненормированные):
coelenterazine -- 2-hydroperoxy-coelenterazine -- Obelia longissima -- Renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.

Держатели документа:
[Antipina, L. Yu
Tomilin, F. N.
Ovchinnikov, S. G.] Russian Acad Sci, LV Kirensky Phys Inst, Siberian Div, Krasnoyarsk, Russia
[Vysotskii, E. S.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Antipina, L. Yu
Ovchinnikov, S. G.] MF Reshetnev Siberian State Aerosp Univ, Krasnoyarsk, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Antipina, L.Y.; Tomilin, F.N.; Vysotskii, E.S.; Ovchinnikov, S.G.

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Sensitivity of Ca2+-regulated photoprotein bioluminescence to magnesium ions is determined by EF-hand motif III / L. P. Burakova, N. P. Malikova, E. S. Vysotski // Luminescence. - 2012. - Vol. 27, Is. 2. - P102-103. - Cited References: 3 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology
Рубрики:
AEQUORIN

Держатели документа:
[Burakova, L. P.
Malikova, N. P.
Vysotski, E. S.] Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Burakova, L.P.; Malikova, N.P.; Vysotski, E.S.

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All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin [Text] / L. . Deng [et al.] // Protein Sci. - 2005. - Vol. 14, Is. 3. - P663-675, DOI 10.1110/ps.041142905. - Cited References: 46 . - ISSN 0961-8368

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   ANGSTROM RESOLUTION
   SEQUENCE-ANALYSIS
   CA2+-REGULATED PHOTOPROTEINS
   CA2+-DISCHARGED PHOTOPROTEIN
   LUMINESCENT PROTEIN
   MODULATED PROTEINS
   ELECTRON-DENSITY
   CLONING
   CDNA
Кл.слова (ненормированные):
bioluminescence -- EF-hand -- fluorescent protein -- proton relay -- calcium-binding loops -- aequorin -- obelin -- diffraction
Аннотация: The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7 Angstrom and 2.2 Angstrom. respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-proteins retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hydroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deng, L...; Vysotski, E.S.; Markova, S.V.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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10.

Crystal structure of a Ca2+-discharged photoprotein - Implications for mechanisms of the calcium trigger and bioluminescence [Text] / L. . Deng [et al.] // J. Biol. Chem. - 2004. - Vol. 279, Is. 32. - P33647-33652, DOI 10.1074/jbc.M402427200. - Cited References: 31 . - ISSN 0021-9258

РУБ Biochemistry & Molecular Biology
Рубрики:
VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   ELECTRON-DENSITY
   W92F OBELIN
   AEQUORIN
   PROTEINS
   LIGHT
   SEQUENCE
   BINDING
   COELENTERAZINE
Аннотация: Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigger and for generation of the different excited states that are the origin of the different colors of bioluminescence. Here we report the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-Angstrom resolution. The results lend support to the proposed mechanisms and provide new structural insight into details of these processes. Global conformational changes caused by Ca2+ association are typical of the class of calcium signal modulators within the EF-hand protein superfamily. Accommodation of the Ca2+ ions into the loops of the EF-hands is seen to propagate into the active site of the protein now occupied by the coelenteramide where there is a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis. Also the H-bonding between His-22 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of coelenteramide, confirming the proposed rapid excited state proton transfer that would lead to the excited state of the phenolate ion pair, which is responsible for the blue emission of bioluminescence.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deng, L...; Markova, S.V.; Vysotski, E.S.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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11.

Preparation and X-ray crystallographic analysis of the Ca2+-discharged photoprotein obelin [Text] / L. . Deng [et al.] // Acta Crystallogr. Sect. D-Biol. Crystallogr. - 2004. - Vol. 60. - P512-514, DOI 10.1107/S090744490302852X. - Cited References: 18 . - ISSN 0907-4449

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Biophysics + Crystallography
Рубрики:
VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   W92F OBELIN
   AEQUORIN
   SEQUENCE
   PROTEIN
   CLONING
   CDNA
Аннотация: Ca2+-regulated photoproteins belong to the EF-hand Ca2+-binding protein family. The addition of calcium ions initiates bright blue bioluminescence of the photoproteins, a result of the oxidative breakdown of coelenterazine peroxide to coelenteramide. Crystals of the Ca2+-discharged W92F mutant of obelin from Obelia longissima have been grown, representing the first crystallization of a photoprotein after the Ca2+-triggered bioluminescence. A green fluorescence observed from the crystals clearly demonstrates that coelenteramide, the bioluminescence product of coelenterazine peroxide, is bound within the protein. The diffraction pattern exhibits tetragonal Laue symmetry. Systematic absences indicate that the space group is either P4(3)2(1)2 or P4(1)2(1)2. The unit-cell parameters are a=b=53.4, c=144.0 Angstrom. The crystals diffract to 1.9 Angstrom resolution.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deng, L...; Markova, S.V.; Vysotski, E.S.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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12.

Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course [Text] / N. G. Berestovskaya [et al.] // Anal. Biochem. - 1999. - Vol. 268, Is. 1. - P72-78, DOI 10.1006/abio.1998.3051. - Cited References: 22 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
Рубрики:
SEQUENCE-ANALYSIS
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   LIGHT-EMISSION
   AEQUORIN
   CDNA
   CLONING
   EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.

Держатели документа:
Russian Acad Sci, Branch Inst Bioorgan Chem, Pushchino 142292, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Tech Univ Berlin, Inst Biochem & Mol Biol, D-10587 Berlin, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Berestovskaya, N.G.; Shaloiko, L.A.; Gorokhovatsky, A.Y.; Bondar, V.S.; Vysotski, E.S.; Maximov, J.E.; von Doehren, H...; Alakhov, Y.B.

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13.

Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state [Text] / Z. J. Liu [et al.] // Proc. Natl. Acad. Sci. U. S. A. - 2006. - Vol. 103, Is. 8. - P2570-2575, DOI 10.1073/pnas.0511142103. - Cited References: 51 . - ISSN 0027-8424

РУБ Multidisciplinary Sciences
Рубрики:
X-RAY-DIFFRACTION
   ANGSTROM RESOLUTION
   CA2+-REGULATED PHOTOPROTEINS
   AEQUORIN BIOLUMINESCENCE
   VIOLET BIOLUMINESCENCE
   W92F OBELIN
   PROTEIN
   LUCIFERASE
   LIGHT
   PROGRAM
Кл.слова (ненормированные):
coelenterazine -- photoprotein -- EF hand -- luciferase -- aequorin
Аннотация: The crystal structure at 1.93-angstrom resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Liu, Z.J.; Stepanyuk, G.A.; Vysotski, E.S.; Lee, J...; Markova, S.V.; Malikova, N.P.; Wang, B.C.

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14.

Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state [Text] / G. A. Stepanyuk [et al.] // BBA-Proteins Proteomics. - 2013. - Vol. 1834, Is. 10. - P2139-2146, DOI 10.1016/j.bbapap.2013.07.006. - Cited References: 64. - This work was supported by RFBR grants 09-04-00172, 12-04-00131, 12-04-91153, and NSFC 31270795 and 31021062, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) "Molecular and Cellular Biology" of the RAS. It was also supported in part with funds from the National Institutes of Health (GM62407), The Georgia Research Alliance and the University of Georgia Research Foundation. Data were collected at Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory. Supporting institutions may be found at www.ser-cat.org/members.html. The use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. W-31-109-Eng-38. . - ISSN 1570-9639

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   COELENTERAZINE-BINDING PROTEIN
   CRYSTAL-STRUCTURE
   MNEMIOPSIS-SP
   CA2+-REGULATED PHOTOPROTEINS
   OBELIN BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   RENILLA-RENIFORMIS
   APO-OBELIN
Кл.слова (ненормированные):
Coelenterazine -- Calcium -- Bioluminescence -- Luciferase
Аннотация: The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca2+-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0 angstrom. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. (C) 2013 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
[Stepanyuk, Galina A.
Liu, Zhi-Jie
Lee, John
Rose, John
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Burakova, Ludmila P.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Liu, Zhi-Jie] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
[Burakova, Ludmila P.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Burakova, L.P.; Lee, J...; Rose, J...; Vysotski, E.S.; Wang, B.C.; RFBR [09-04-00172, 12-04-00131, 12-04-91153]; NSFC [31270795, 31021062]; Government of Russian Federation of the RAS [11.G34.31.0058]; National Institutes of Health [GM62407]; Georgia Research Alliance; University of Georgia Research Foundation; U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]

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15.

CADMIUM-INDUCED LUMINESCENCE OF RECOMBINANT PHOTOPROTEIN OBELIN [Text] / V. S. BONDAR [et al.] // Biochim. Biophys. Acta-Bioenerg. - 1995. - Vol. 1231, Is. 1. - P29-32, DOI 10.1016/0005-2728(95)00059-R. - Cited References: 21 . - ISSN 0005-2728

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
AEQUORIN
Кл.слова (ненормированные):
PHOTOPROTEIN -- OBELIN -- CADMIUM -- BIOLUMINESCENCE
Аннотация: It has been shown for the first time that Cd2+ ions induce substantial bioluminescence of a Ca2+-binding photoprotein: recombinant obelin. The optimum pH for the bioluminescent rr:action in the presence of Cd2+ ions is pH 6. The intensity, L, of the light emission for the Cd2+ ions is 75% of the intensity of the signal in the presence of Ca2+. The quantum yields of the reactions in the presence of Cd2+ and Ca2+ are 0.18 and 0.24 respectively. The slope of the straight line (between 5 and 90% of L,,) in the coordinates of log(L/(L(max) - L)) vs. log([Cd2+]) is 1.75 +/- 0.06, which indicates positive cooperative character of this reaction. At a concentration exceeding 1 . 10(-3) M, Cd2+ inhibits the bioluminescent reaction.

Держатели документа:
AGR UNIV WAGENINGEN,DEPT BIOCHEM,6703 HA WAGENINGEN,NETHERLANDS
RUSSIAN ACAD SCI,INST BIOPHYS,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; SERGEEV, A.G.; ILLARIONOV, B.A.; VERVOORT, J...; HAGEN, W.R.

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16.

Effect of different salts and detergents on luciferin-luciferase luminescence of the enchytraeid Fridericia heliota / N. S. Rodionova, V. N. Petushkov // Journal of Photochemistry and Photobiology B: Biology. - 2006. - Vol. 83, Is. 2. - P123-128, DOI 10.1016/j.jphotobiol.2005.12.014 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Ions -- Luciferin-luciferase systems -- Triton X-100 -- adenosine triphosphate -- anion -- bromine -- calcium ion -- carbonic acid -- cation -- chloride -- chromium derivative -- detergent -- dodecyl sulfate sodium -- inorganic salt -- iodine -- iron derivative -- luciferase -- luciferin -- magnesium ion -- manganese -- nitrate -- phosphate -- sulfate -- sulfite -- triton x 100 -- annelid worm -- article -- bioluminescence -- concentration (parameters) -- controlled study -- enzyme activation -- enzyme activity -- enzyme inhibition -- enzyme mechanism -- in vitro study -- nonhuman -- priority journal -- qualitative analysis -- quantitative analysis -- Adenosine Triphosphate -- Animals -- Cations, Divalent -- Cations, Monovalent -- Detergents -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescence -- Metals -- Oligochaeta -- Photobiology -- Salts -- Annelida -- Clitellata -- earthworms (sp.) -- Enchytraeidae -- Fridericia heliota -- Oligochaeta (Metazoa) -- Pheretima sieboldi
Аннотация: The study addresses the effect produced by different inorganic salts and detergents (SDS, Triton X-100, the Tween series) on the ATP-dependent bioluminescent reaction catalyzed by the luciferase of the new earthworm species Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae). It has been shown that the effect of divalent metal salts on luminescence is determined by the action of cations. Three of them - Mg2+, Mn2+ and Ca2+ - can stimulate luciferase activity at concentrations varying within a wide range, and Mn2+ can act as a 100%-effective substitute for Mg2+ in F. heliota luminescence reaction in vitro. The inhibitory effect of monovalent metal salts on luminescence is largely determined by the action of the anion part of the molecule. The effectiveness of the inhibitory effect of anions increases in the following order: {Mathematical expression}. Of the sodium salts, dodecyl sulfate, which is an anionic detergent, produces the strongest inhibitory effect on luciferase. On the contrary, nonionic detergents produce a stimulatory effect on the F. heliota luciferase. The action of the most effective of them - Triton X-100 - is determined by its ability to reduce the actual concentration of lipid inhibitors in the reaction mixture. В© 2006 Elsevier B.V. All rights reserved.

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

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

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17.

ELECTROPHORETIC BEHAVIOR OF HYDROSOLS OF ULTRADISPERSE DIAMOND AND MODIFICATION OF ITS SURFACE [Text] / G. A. CHIGANOVA, V. A. BONDAR, A. S. CHIGANOV // COLLOID JOURNAL OF THE RUSSIAN ACADEMY OF SCIENCES. - 1993. - Vol. 55, Is. 5. - P. 774-775. - Cited References: 5 . - ISSN 1061-933X

РУБ Chemistry, Physical

Аннотация: The method of macro-electrophoresis is used to determine values of the zeta-potential of particles of ultradisperse diamond in solutions of AlCl3. It is shown that an increase in the concentration of aluminum ions to 0.5.10(-4) M leads to a decrease in the negative charge of the diamond particles; the dispersions coagulate in more concentrated solutions of AlCl3. Chemical modification of the surface of ultradisperse diamond by aluminum ions is used to obtain stable hydrosols with positively charged diamond particles.

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

Доп.точки доступа:
CHIGANOVA, G.A.; BONDAR, V.A.; CHIGANOV, A.S.

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18.

Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course [Text] / N. G. Berestovskaya [et al.] // Anal. Biochem. - 1999. - Vol. 268, Is. 1. - P. 72-78, DOI 10.1006/abio.1998.3051. - Cited References: 22 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
Рубрики:
SEQUENCE-ANALYSIS
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   LIGHT-EMISSION
   AEQUORIN
   CDNA
   CLONING
   EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.

WOS
Держатели документа:
Russian Acad Sci, Branch Inst Bioorgan Chem, Pushchino 142292, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Tech Univ Berlin, Inst Biochem & Mol Biol, D-10587 Berlin, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Berestovskaya, N.G.; Shaloiko, L.A.; Gorokhovatsky, A.Y.; Bondar, V.S.; Vysotski, E.S.; Maximov, J.E.; von Doehren, H...; Alakhov, Y.B.

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19.

Expression of lux-genes as an indicator of metabolic activity of cells in model ecosystem studies [Text] / A. N. Boyandin, L. Y. Popova ; ed. M Nelson [et al.] // SPACE LIFE SCIENCES: CLOSED ARTIFICIAL ECOSYSTEMS AND LIFE SUPPORT SYSTEMS. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON-ELSEVIER SCIENCE LTD, 2003. - Vol. 31: Meeting of F4 1 Session of the 34th Scientific Assembly of COSPAR (OCT, 2002, HOUSTON, TEXAS), Is. 7. - P. 1839-1845, DOI 10.1016/S0273-1177(03)00014-0. - Cited References: 8 . - ISBN 0273-1177

РУБ Engineering, Aerospace + Astronomy & Astrophysics + Ecology + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

Аннотация: Quick response to different impacts and easy measurement make the luminescent systems of luminous bacteria an object convenient for application in various fields. Cloning of gene luminescence in different organisms is currently used to study both the survival of microbial cells and the effect of different factors on their metabolic activity, including the environment. A primary test-object in estimating bacteriological contamination of water bodies, Escherichia coli, can be conveniently used as an indicator of bactericidal properties of aquatic ecosystems. The application of Escherichia coli Z905/pPHL7 (lux(+)) as a marker microorganism can facilitate monitoring the microbiological status of closed biocenoses, including systems with higher organisms. The investigation of various parameters of microecosystems (carbon nutrition type, concentrations of inorganic ions and toxic compounds) shows that the recombinant strain E. coli Z905/pPHL7 can be effectively used as a marker. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

WOS
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:
Boyandin, A.N.; Popova, L.Y.; Nelson, M \ed.\; Pechurkin, NS \ed.\; Dempster, WF \ed.\; Somova, LA \ed.\; Somo, , LA \ed.\

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20.

Biofilm formation by bacterial associations under various salinities and copper ion stress [Text] / O. A. Mogilnaya [et al.] // Biofouling. - 2005. - Vol. 21, Is. 05.06.2013. - P. 247-255, DOI 10.1080/08924010500445848. - Cited References: 24 . - ISSN 0892-7014

РУБ Biotechnology & Applied Microbiology + Marine & Freshwater Biology
Рубрики:
HEAVY-METAL RESISTANCE
   BACILLUS-SUBTILIS
   PROTEIN
   RISK
Кл.слова (ненормированные):
binary community -- surface films -- adhesion -- copper -- stress
Аннотация: The study addresses the effect of abiotic (medium salinity and copper ions) and biotic (interactions between populations) factors on the formation of structured communities by binary associations consisting of halotolerant bacteria (Alcaligenes sp. 1-1 or Acinetobacter sp. 1-19) and a wild-type B. subtilis 2335 strain or a transgenic strain. The results showed that 250 mg l(-1) of copper ions inhibit formation of biofilms by monocultures of the tested strains. Binary associations of the strains were more resistant to high concentrations (250 mg l(-1)) of copper ions. At the lowest NaCl concentration (0.05% and 2.5%) and in the presence of copper ions, bacilli seemed to help halotolerant bacteria survive. Under increased salinity and in the presence of copper ions, structured communities developed due to halotolerant bacteria. Coexistence under stressful conditions was beneficial for the both groups of bacteria.

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

Доп.точки доступа:
Mogilnaya, O.A.; Lobova, T.I.; Kargatova, T.V.; Popova, L.Y.

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