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Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species [Text] / E. S. Vysotski [et al.] // Biochemistry. - 2003. - Vol. 42, Is. 20. - P6013-6024, DOI 10.1021/bi027258h. - Cited References: 45 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CALCIUM
   LUMINESCENCE
   LONGISSIMA
   EVOLUTION
   PROTEINS
   COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA USA
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia
Univ Washington, Friday Harbor Labs, Seattle, WA 98195 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Liu, Z.J.; Markova, S.V.; Blinks, J.R.; Deng, L...; Frank, L.A.; Herko, M...; Malikova, N.P.; Rose, J.P.; Wang, B.C.; Lee, J...

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Utilization of substrate when growing oyster mushroom Pleurotus florida Fovose [Текст] / N. S. Manukovsky, V. S. Kovalev, I. V. Gribovskaya // Mikol. Fitopatol. - 1998. - Vol. 32, Is. 6. - P. 43-46. - Cited References: 8 . - ISSN 0026-3648

РУБ Mycology

Аннотация: Content of biogenic elements in the residual substrate after growing of oyster mushroom Pleurotus florida Fovose on wheat straw was studied. It was calculated, that masses of sulphur, calcium and magnesium in the residual substrate were more than 90 % of their initial masses in wheat straw used for growing. Therefore the accumulation of these elements in the substrate under its repeated recycling for mushroom growing is possible. On the contrary the lack of phosphorus is expected. After washing content of all biogenic elements tested in residual substrate, except for calcium, was lower than their content in wheat straw. The decreasing of mushroom yield under increasing rate of residual substrate in its mixture with wheat straw was shown. Washing of residual substrate did not lead to decreasing of yield.

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

Доп.точки доступа:
Manukovsky, N.S.; Kovalev, V.S.; Gribovskaya, I.V.

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The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein / S. V. Markova [et al.] // FEBS J. - 2012. - Vol. 279, Is. 5. - P856-870, DOI 10.1111/j.1742-4658.2012.08476.x. - Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany). . - ISSN 1742-464X

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   C-TERMINAL PROLINE
   SEQUENCE-ANALYSIS
   MNEMIOPSIS-SP
   COELENTERAZINE-BINDING
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURES
   EXCITED-STATE
   CDNA CLONING
Кл.слова (ненормированные):
bioluminescence -- calcium -- coelenterazine -- luciferase -- mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Malikova, Natalia P.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Dept Biophys, Krasnoyarsk, Russia
[Golz, Stefan] Bayer Pharma AG, Global Drug Discovery, Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Golz, S...; Malikova, N.P.; Frank, L.A.; Vysotski, E.S.

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The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding [Text] / E. V. Eremeeva [et al.] // FEBS Lett. - 2009. - Vol. 583, Is. 12. - P1939-1944, DOI 10.1016/j.febslet.2009.04.043. - Cited References: 28. - We thank Prof. John Lee for valuable suggestions and providing constructive criticisms. The work was supported by Wageningen University Sandwich PhD-Fellowship Program, Grants 02.512.12. 2006 and 1211.2008.4 of Ministry of Education and Science of Russian Federation, MCB Program of RAS, and by Grant No. 2 of SB RAS. . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
CRYSTAL-STRUCTURE
   CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   CALCIUM
   REGENERATION
   APOAEQUORIN
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Photoprotein -- Trp fluorescence
Аннотация: The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Westphal, Adrie H.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Westphal, A.H.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.; Wageningen University Sandwich PhD-Fellowship Program [02.512.12. 2006]; Ministry of Education and Science of Russian Federation, MCB Program of RAS [1211.2008.4]; SB RAS

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The effect of deicing salt solutes on Moina macrocopa and Allium cepa in a toxicity test experiment / T. S. Lopatina, Y. V. Aleksandrova, O. V. Anishchenko [и др.] // Vestn. Tomsk. Gos. Univ. Biol. - 2020. - Is. 51. - С. 162-178, DOI 10.17223/19988591/51/9 . - ISSN 1998-8591
Кл.слова (ненормированные):
Aquatic ecosystems -- Cladocera, Allium-test -- Salinity -- Toxicity test
Аннотация: Chloride salts are the most commonly used deicing materials for winter maintenance of roads. Numerous studies indicate a significant increase in the salinity of aquatic ecosystems associated with the long-term use of deicing materials in countries located in cold climates. The functioning of ecosystems largely depends on salinity, since salinity is one of the key factors determining the species composition, the structure of food webs and the productivity of aquatic communities. Given the growing threat of salinization of groundwater and surface waters, it is extremely important to study the effect of deicing materials on the biota and functioning of aquatic ecosystems. The aim of this research is to determine the threshold concentrations of solutions of the deicing salt mixture “Bionord” containing sodium and calcium chlorides, at which negative effects on the development of animal and plant test objects are observed. In this study, we used the salt-containing mixture “Bionord” as a model deicer. Similarly, with the most commonly used ice melting chemicals, the «Bionord» salt mixture contains a large amount of sodium and calcium chlorides (about 85% of the total weight). To evaluate the toxicity of the deicer solutions, we used acute and chronic toxicity tests with cladoceran Moina macrocopa (Straus, 1820) (Cladocera: Moinidae) and standard onion-based test with Allium cepa L. (Liliopsida: Amaryllidaceae) (Allium-test). In acute and chronic toxicity tests with Cladocera, the females on the first day of their life (body size 0.5-0.6 mm) were placed individually in jars with aged (not less than for 72 h) tap water with a volume of 20 ml with the addition of a deicer at a certain concentration. A group of animals that was placed in the medium without the deicer was used as a control. In the acute toxicity tests, we used the following concentration of the deicer: 1.3; 2.5; 4.0, 5.0; 6.0; 8.0; 10.0 g/l. The mortality of animals was recorded 24 and 48 hours after the start of the experiment. The concentration of the deicer (LC50) at which 50% of animals was observed to die, compared to the control, was determined in the acute toxicity test. In a chronic toxicity test, animals were tested in the following range of concentrations of the deicer: 0.3; 0.6; 1.3; 2.5; 5.0; 6.0 and 8.0 g/l. The chronic toxicity test was conducted until the death of all test animals. Based on the data obtained in the chronic toxicity test, the specific growth rate of juvenile females, average fecundity, and average life span of M. macrocopa were calculated for each concentration of the deicer. Bulbs of onions of the Stuttgartenrisen variety with a diameter of 1.8 ± 0.1 cm and a weight of 2.27 ± 0.17 g were used in the onion test. Bulbs with their bottoms were placed in test tubes containing 20 ml of a solute of the deicer or tap water for 48 hours. Three bulbs were tested for each concentration and for the control. The following concentrations of the deicer were used in the onion test: 1.0; 2.5; 5.0; 7.0; 10.0; 15.0; 20.0; 50.0 g/l. The general toxic and cytotoxic effects were evaluated in the onion test. The average root length and the total root length on each bulb were used as indicators of the total toxicity of the solutions of deicer. To evaluate proliferative activity, we calculated the mitotic index as the fraction of dividing cells in the apical root meristem to the total number of cells. Based on the results of the experiments, we determined median effective mixture concentrations (EC50) at which there is a 50% decrease, compared to the control, in the values of root growth indicators: average root length, sum of root lengths on each bulb and mitotic index. Median lethal concentration (LC50) of the deicing salt determined in the 48-hour acute toxicity test with females of M. macrocopa was equal to 5.1 g/l. In the chronic test, we showed that the exposure to the solutions of the deicing salt in the range of concentrations from 0.3 to 5.0 g/l does not affect the life span, specific growth rate of juveniles and fecundity of females of M. macrocopa. The median effective concentration (EC50) of the deicing salt determined in the Allium-tests were 6.3, 5.2 and 10.4 g/l for the sum of root lengths, average root length on each bulb and proliferative activity at the tips of roots (mitotic index), respectively (See Table 1 and 2). Complete inhibition of onion root growth was observed at the concentration of the decider equal to 20 g/l, while the death of all test animals in the acute toxicity test occurred at the concentration of the deicer equal to 8,0 g/l (See Fig. 1). Thus, we demonstrated that similar concentrations of the deicer induced 50% inhibition of the growth of onion roots and 50% mortality of cladocerans. These values, in general, corresponded to a critical salinity of 5-8 % above which qualitative changes occur both in the external and internal condition of aquatic animals. The electrical conductivity of the deicer solutions, which had a negative effect on the selected test species, coincides with the previously obtained values of the electrical conductivity of sodium chloride solutions harmful to cladocerans. We can assume that the main mechanism of the effect of the deicing material that we study is associated with the biological effect of its chlorine and sodium salts. Taking this into account, the value of electrical conductivity measured for solutions of deicing salt can be used to assess its negative potential effects. We estimated that in the absence of timely cleaning, regulated by the rules for using the material, the runoff from each square meter of the treated surface can lead to the pollution of 8-13 liters of fresh water. Thus, the basic requirement for the use of deicing salts on roads is the need to comply with the cleaning regime of the treated surfaces. Otherwise, the gradual accumulation of sodium and calcium chlorides in water bodies can cause an increase in salinity which will affect the survival of freshwater aquatic organisms and lead to serious disturbances in the functioning of aquatic ecosystems. © 2020 Tomsk State University. All rights reserved.

Scopus
Держатели документа:
Laboratory of Ecosystem Biophysics, Institute of Biophysics, Federal Research Centre Krasnoyarsk Scientific Centre, Siberian Branch, Russian Academy of Sciences, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Laboratory of Bioluminescent and Environmental Technologies, Institute of Biophysics, Federal Research Centre Krasnoyarsk Scientific Centre, Siberian Branch, Russian Academy of Sciences, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Analytical Laboratory, Institute of Biophysics, Federal Research Centre Krasnoyarsk Scientific Centre, Siberian Branch, Russian Academy of Sciences, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Department of Biophysics, School of Fundamental Biology and Biotechnology, Siberian Federal University, 79 Svobodniy Ave, Krasnoyarsk, 660041, Russian Federation
Laboratory of Ecosystem Biophysics, Institute of Biophysics, Federal Research Centre Krasnoyarsk Scientific Centre, Siberian Branch, Russian Academy of Sciences, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Lopatina, T. S.; Aleksandrova, Y. V.; Anishchenko, O. V.; Gribovskaya, I. V.; Oskina, N. A.; Zotina, T. A.; Zadereev, E. S.

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РУБ Biology + Ecology
Рубрики:
DAPHNIA-MAGNA
   NACL SALINITY
   ROAD SALTS
   WATER
   FRESH
   CHLORIDE
Кл.слова (ненормированные):
salinity -- toxicity test -- Cladocera -- Allium-test -- aquatic ecosystems
Аннотация: Chloride salts are the most commonly used deicing materials for winter maintenance of roads. Numerous studies indicate a significant increase in the salinity of aquatic ecosystems associated with the long-term use of deicing materials in countries located in cold climates. The functioning of ecosystems largely depends on salinity, since salinity is one of the key factors determining the species composition, the structure of food webs and the productivity of aquatic communities. Given the growing threat of salinization of groundwater and surface waters, it is extremely important to study the effect of deicing materials on the biota and functioning of aquatic ecosystems. The aim of this research is to determine the threshold concentrations of solutions of the deicing salt mixture "Bionord" containing sodium and calcium chlorides, at which negative effects on the development of animal and plant test objects are observed. In this study, we used the salt-containing mixture "Bionord" as a model deicer. Similarly, with the most commonly used ice melting chemicals, the "Bionord" salt mixture contains a large amount of sodium and calcium chlorides (about 85% of the total weight). To evaluate the toxicity of the deicer solutions, we used acute and chronic toxicity tests with cladoceran Moina macrocopa (Straus, 1820) (Cladocera: Moinidae) and standard onion-based test with Allium cepa L. (Liliopsida: Amaryllidaceae) (Allium-test). In acute and chronic toxicity tests with Cladocera, the females on the first day of their life (body size 0.5-0.6 mm) were placed individually in jars with aged (not less than for 72 h) tap water with a volume of 20 ml with the addition of a deicer at a certain concentration. A group of animals that was placed in the medium without the deicer was used as a control. In the acute toxicity tests, we used the following concentration of the deicer: 1.3; 2.5; 4.0, 5.0; 6.0; 8.0; 10.0 g/l. The mortality of animals was recorded 24 and 48 hours after the start of the experiment. The concentration of the deicer (LC50) at which 50% of animals was observed to die, compared to the control, was determined in the acute toxicity test. In a chronic toxicity test, animals were tested in the following range of concentrations of the deicer: 0.3; 0.6; 1.3; 2.5; 5.0; 6.0 and 8.0 g/l. The chronic toxicity test was conducted until the death of all test animals. Based on the data obtained in the chronic toxicity test, the specific growth rate of juvenile females, average fecundity, and average life span of M. macrocopa were calculated for each concentration of the deicer. Bulbs of onions of the Stuttgartenrisen variety with a diameter of 1.8 +/- 0.1 cm and a weight of 2.27 +/- 0.17 g were used in the onion test. Bulbs with their bottoms were placed in test tubes containing 20 ml of a solute of the deicer or tap water for 48 hours. Three bulbs were tested for each concentration and for the control. The following concentrations of the deicer were used in the onion test: 1.0; 2.5; 5.0; 7.0; 10.0; 15.0; 20.0; 50.0 g/l. The general toxic and cytotoxic effects were evaluated in the onion test. The average root length and the total root length on each bulb were used as indicators of the total toxicity of the solutions of deicer. To evaluate proliferative activity, we calculated the mitotic index as the fraction of dividing cells in the apical root meristem to the total number of cells. Based on the results of the experiments, we determined median effective mixture concentrations (EC50) at which there is a 50% decrease, compared to the control, in the values of root growth indicators: average root length, sum of root lengths on each bulb and mitotic index. Median lethal concentration (LC50) of the deicing salt determined in the 48-hour acute toxicity test with females of Al. macrocopa was equal to 5.1 g/l. In the chronic test, we showed that the exposure to the solutions of the deicing salt in the range of concentrations from 0.3 to 5.0 g/l does not affect the life span, specific growth rate of juveniles and fecundity of females of M. macrocopa. The median effective concentration (EC50) of the deicing salt determined in the Allium-tests were 6.3, 5.2 and 10.4 g/l for the sum of root lengths, average root length on each bulb and proliferative activity at the tips of roots (mitotic index), respectively (See Table 1 and 2). Complete inhibition of onion root growth was observed at the concentration of the decider equal to 20 g/l, while the death of all test animals in the acute toxicity test occurred at the concentration of the deicer equal to 8,0 g/l (See Fig. 1). Thus, we demonstrated that similar concentrations of the deicer induced 50% inhibition of the growth of onion roots and 50% mortality of cladocerans. These values, in general, corresponded to a critical salinity of 5-8 %o above which qualitative changes occur both in the external and internal condition of aquatic animals. The electrical conductivity of the deicer solutions, which had a negative effect on the selected test species, coincides with the previously obtained values of the electrical conductivity of sodium chloride solutions harmful to cladocerans. We can assume that the main mechanism of the effect of the deicing material that we study is associated with the biological effect of its chlorine and sodium salts Taking this into account, the value of electrical conductivity measured for solutions of deicing salt can be used to assess its negative potential effects. We estimated that in the absence of timely cleaning, regulated by the rules for using the material, the runoff from each square meter of the treated surface can lead to the pollution of 8-13 liters of fresh water. Thus, the basic requirement for the use of deicing salts on roads is the need to comply with the cleaning regime of the treated surfaces. Otherwise, the gradual accumulation of sodium and calcium chlorides in water bodies can cause an increase in salinity which will affect the survival of freshwater aquatic organisms and lead to serious disturbances in the functioning of aquatic ecosystems.

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Держатели документа:
Russian Acad Sci, Fed Res Ctr, Inst Biophys, Siberian Branch,Krasnoyarsk Sci Ctr,Lab Ecosyst B, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Fed Res Ctr, Inst Biophys, Siberian Branch,Krasnoyarsk Sci Ctr,Lab Biolumine, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Fed Res Ctr, Inst Biophys, Siberian Branch,Krasnoyarsk Sci Ctr,Analyt Lab, 50-50 Akademgorodok, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Dept Biophys, 79 Svobodniy Ave, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Lopatina, Tatiana S.; Aleksandrova, Yuliyana, V; Anishchenko, Olesya, V; Gribovskaya, Iliada, V; Oskina, Nataliya A.; Zotina, Tatiana A.; Zadereev, Egor S.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR); Government of Krasnoyarsk Krai; Krasnoyarsk Krai Fund for Supporting Scientific and Scientific-Technical Activities [19-44-240014]

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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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Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction [Text] / P. V. Natashin [et al.] // Acta Crystallogr. Sect. D-Biol. Crystallogr. - 2014. - Vol. 70. - P720-732, DOI 10.1107/S1399004713032434. - Cited References: 71. - We acknowledge the use of beamline BL17U1 at the Shanghai Synchrotron Radiation Facility, China. This work was supported by RFBR grants 12-04-91153, 12-04-00131 and the China-Russia International Collaboration grant from the Chinese Academy of Sciences and NSFC, by the Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' (grant 11.G34.31.0058) and 'Molecular and Cellular Biology' of the RAS, the President of the Russian Federation 'Leading Science School' (grant 3951.2012.4). PVN and EVE were supported by RFBR grant 14-04-31092. . - ISSN 0907-4449. - ISSN 1399-0047

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Biophysics + Crystallography
Рубрики:
AEQUORIN BIOLUMINESCENCE
   SEQUENCE-ANALYSIS
   CRYSTAL-STRUCTURE
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   CALCIUM CONCENTRATION
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MNEMIOPSIS-LEIDYI
   EXCITED-STATES
Аннотация: Ca2+-regulated photoproteins, which are responsible for light emission in a variety of marine coelenterates, are a highly valuable tool for measuring Ca2+ inside living cells. All of the photoproteins are a single-chain polypeptide to which a 2-hydroperoxycoelenterazine molecule is tightly but noncovalently bound. Bioluminescence results from the oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. Here, the crystal structures of the Y138F obelin mutant before and after bioluminescence are reported at 1.72 and 1.30 angstrom resolution, respectively. The comparison of the spatial structures of the conformational states of Y138F obelin with those of wild-type obelin gives clear evidence that the substitution of Tyr by Phe does not affect the overall structure of both Y138F obelin and its product following Ca2+ discharge compared with the corresponding conformational states of wild-type obelin. Despite the similarity of the overall structures and internal cavities of Y138F and wild-type obelins, there is a substantial difference: in the cavity of Y138F obelin a water molecule corresponding to W2 in wild-type obelin is not found. However, in Ca2+-discharged Y138F obelin this water molecule now appears in the same location. This finding, together with the observed much slower kinetics of Y138F obelin, clearly supports the hypothesis that the function of a water molecule in this location is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion before its decomposition into the excited-state product. Although obelin differs from other hydromedusan Ca2+-regulated photoproteins in some of its properties, they are believed to share a common mechanism.

wos
Держатели документа:
[Natashin, Pavel V.
Ding, Wei
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Chair Biophys, Krasnoyarsk, Russia
[Ding, Wei] Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, Beijing 100080, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem Mol Biol, Athens, GA 30602 USA
[Liu, Zhi-Jie] Shanghai Tech Univ, Human Inst, Shanghai, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Ding, W...; Eremeeva, E.V.; Markova, S.V.; Lee, J...; Vysotski, E.S.; Liu, Z.J.; RFBR [12-04-91153, 12-04-00131, 14-04-31092]; Chinese Academy of Sciences; NSFC; Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' [11.G34.31.0058]; RAS; Russian Federation 'Leading Science School' [3951.2012.4]

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Structure of the Ca2+-regulated photoprotein obelin at 1.7 angstrom resolution determined directly from its sulfur substructure [Text] / Z. J. Liu [et al.] // Protein Sci. - 2000. - Vol. 9, Is. 11. - P2085-2093. - Cited References: 41 . - ISSN 0961-8368

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-MODULATED PROTEINS
   AMINO-ACID SEQUENCE
   CA-2+-BINDING PHOTOPROTEIN
   CA2+-BINDING PHOTOPROTEIN
   MACROMOLECULAR STRUCTURES
   3-DIMENSIONAL STRUCTURE
   ANOMALOUS SCATTERING
   CRYSTAL-STRUCTURES
   DIFFRACTION DATA
   BINDING SITE
Кл.слова (ненормированные):
bioluminescence -- crystallography -- obelin -- photoprotein -- single wavelength anomalous scattering -- solvent flattening -- sulfur phasing
Аннотация: The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 Angstrom resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.

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

Доп.точки доступа:
Liu, Z.J.; Vysotski, E.S.; Chen, C.J.; Rose, J.P.; Lee, J...; Wang, B.C.

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10.

Structure based mechanism of the Ca2+ -induced release of coelenterazine from the Renilla binding protein [Text] / G. A. Stepanyuk [et al.] // Proteins. - 2009. - Vol. 74, Is. 3. - P583-593, DOI 10.1002/prot.22173. - Cited References: 26 . - ISSN 0887-3585

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
   CRYSTAL-STRUCTURES
   RENIFORMIS
   LUCIFERASE
   BIOLUMINESCENCE
   PURIFICATION
   ANGSTROM
   MUELLERI
Кл.слова (ненормированные):
bioluminescence -- EF-hand -- coelenteramider -- luciferase -- Ca2+-binding protein
Аннотация: The crystal structure of the Ca2+-loaded coelenterazine binding protein from Renilla muelleri in its apo-state has been determined at resolution 1.8 angstrom. Although calcium binding hardly affects the compact scaffold and overall fold of the structure before calcium addition, there are easily discerned shifts in the residues that were interacting with the coelenterazine and a repositioning of helices, to expose a cavity to the external solvent. Altogether these changes offer a straightforward explanation for how following the addition of Ca2+, the coelenterazine could escape and become available for bioluminescence on Renilla luciferase. A docking computation supports the possibility of a luciferase-binding protein complex.

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

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

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11.

Structural basis for the emission of violet bioluminescence from a W92F obelin mutant [Text] / L. . Deng [et al.] // FEBS Lett. - 2001. - Vol. 506, Is. 3. - P281-285, DOI 10.1016/S0014-5793(01)02937-4. - Cited References: 15 . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
AEQUORIN
Кл.слова (ненормированные):
calcium-regulated photoprotein -- X-ray crystallography -- fluorescence -- coelenterazine -- aequorin
Аннотация: Mutation of the Trp92 that is known to lie within the active site of the photoprotein obelin from Obelia longissima, results in a shift of the bioluminescence color from blue (lambda (max) = 485 nm) to violet. The corrected spectrum shows a new band with lambda (max) = 410 nm now contributing equally to the one at longer wavelength. The crystal structure of this W92F obelin determined at 1.72 Angstrom resolution shows that there is no significant change in the dimensions of the active site between WT obelin (recombinant Ca2+-regulated photoprotein from Obelia longissima) and the mutant. It is proposed that the bioluminescence spectral shift results from removal of a hydrogen bond from the indole of W92 nearby a hydroxyl belonging to the 6-phenyl substituent of the substrate coelenterazine. Propagation of fbis change through a conjugated bond system in the excited state of the product coelenteramide affects the coupling of the N1-position and the hydrogen-bonded Y138. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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12.

Spectral tuning of obelin bioluminescence by mutations of Trp92 [Text] / N. P. Malikova [et al.] // FEBS Lett. - 2003. - Vol. 554, Is. 01.02.2013. - P184-188, DOI 10.1016/S0014-5793(03)01166-9. - Cited References: 13 . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
VIOLET BIOLUMINESCENCE
   W92F OBELIN
   AEQUORIN
   PURIFICATION
   EXPRESSION
   EMISSION
   CLONING
Кл.слова (ненормированные):
photoprotein -- aequorin -- calcium -- fluorescence
Аннотация: The Ca2+-regulated photoprotein obelin was substituted at Trp92 by His, Lys, Glu, and Arg. All mutants fold into stable conformations and produce bimodal bioluminescence spectra with enhanced contribution from a violet emission. The W92R mutant has an almost monomodal bioluminescence (lambda(max)=390 nm) and monomodal fluorescence (lambda(max)=425 nm) of the product. Results are interpreted by an excited state proton transfer mechanism involving the substituent side group and His22 in the binding cavity. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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

Доп.точки доступа:
Malikova, N.P.; Stepanyuk, G.A.; Frank, L.A.; Markova, S.V.; Vysotski, E.S.; Lee, J...

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13.

Specific Activities of Hydromedusan Ca2+-Regulated Photoproteins / N. P. Malikova, E. V. Eremeeva, D. V. Gulnov [et al.] // Photochem. Photobiol. - 2021, DOI 10.1111/php.13556 . - Article in press. - ISSN 0031-8655
Аннотация: Nowadays the recombinant Ca2+-regulated photoproteins originating from marine luminous organisms are widely applied to monitor calcium transients in living cells due to their ability to emit light on Ca2+ binding. Here we report the specific activities of the recombinant Ca2+-regulated photoproteins—aequorin from Aequorea victoria, obelins from Obelia longissima and Obelia geniculata, clytin from Clytia gregaria and mitrocomin from Mitrocoma cellularia. We demonstrate that along with bioluminescence spectra, kinetics of light signals and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of bioluminescent reactions. The highest specific activities were found for obelins and mitrocomin, whereas those of aequorin and clytin were shown to be lower. To determine the factors influencing the variations in specific activities the fluorescence quantum yields for Ca2+-discharged photoproteins were measured and found to be quite different varying in the range of 0.16–0.36. We propose that distinctions in specific activities may result from different efficiencies of singlet excited state generation and different fluorescence quantum yields of coelenteramide bound within substrate-binding cavity. This in turn may be conditioned by variations in the amino acid environment of the substrate-binding cavities and hydrogen bond distances between key residues and atoms of 2-hydroperoxycoelenterazine. © 2021 American Society for Photobiology

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

Доп.точки доступа:
Malikova, N. P.; Eremeeva, E. V.; Gulnov, D. V.; Natashin, P. V.; Nemtseva, E. V.; Vysotski, E. S.

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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.

Spatial and temporal variation in Arctic freshwater chemistry—Reflecting climate-induced landscape alterations and a changing template for biodiversity / B. J. Huser, M. N. Futter, D. Bogan [et al.] // Freshw. Biol. - 2020, DOI 10.1111/fwb.13645 . - Article in press. - ISSN 0046-5070
Кл.слова (ненормированные):
biogeochemistry -- eutrophication -- lakes -- oligotrophication -- rivers
Аннотация: Freshwater chemistry across the circumpolar region was characterised using a pan-Arctic data set from 1,032 lake and 482 river stations. Temporal trends were estimated for Early (1970–1985), Middle (1986–2000), and Late (2001–2015) periods. Spatial patterns were assessed using data collected since 2001. Alkalinity, pH, conductivity, sulfate, chloride, sodium, calcium, and magnesium (major ions) were generally higher in the northern-most Arctic regions than in the Near Arctic (southern-most) region. In particular, spatial patterns in pH, alkalinity, calcium, and magnesium appeared to reflect underlying geology, with more alkaline waters in the High Arctic and Sub Arctic, where sedimentary bedrock dominated. Carbon and nutrients displayed latitudinal trends, with lower levels of dissolved organic carbon (DOC), total nitrogen, and (to a lesser extent) total phosphorus (TP) in the High and Low Arctic than at lower latitudes. Significantly higher nutrient levels were observed in systems impacted by permafrost thaw slumps. Bulk temporal trends indicated that TP was higher during the Late period in the High Arctic, whereas it was lower in the Near Arctic. In contrast, DOC and total nitrogen were both lower during the Late period in the High Arctic sites. Major ion concentrations were higher in the Near, Sub, and Low Arctic during the Late period, but the opposite bulk trend was found in the High Arctic. Significant pan-Arctic temporal trends were detected for all variables, with the most prevalent being negative TP trends in the Near and Sub Arctic, and positive trends in the High and Low Arctic (mean trends ranged from +0.57%/year in the High/Low Arctic to ?2.2%/year in the Near Arctic), indicating widespread nutrient enrichment at higher latitudes and oligotrophication at lower latitudes. The divergent P trends across regions may be explained by changes in deposition and climate, causing decreased catchment transport of P in the south (e.g. increased soil binding and trapping in terrestrial vegetation) and increased P availability in the north (deepening of the active layer of the permafrost and soil/sediment sloughing). Other changes in concentrations of major ions and DOC were consistent with projected effects of ongoing climate change. Given the ongoing warming across the Arctic, these region-specific changes are likely to have even greater effects on Arctic water quality, biota, ecosystem function and services, and human well-being in the future. © 2020 The Authors. Freshwater Biology published by John Wiley & Sons Ltd.

Scopus
Держатели документа:
Department of Aquatic Sciences and Assessment, Swedish University of Agricultural Sciences, Uppsala, Sweden
Alaska Center for Conservation Science, University of Alaska Anchorage, Anchorage, AK, United States
Norwegian Water Resources & Energy Directorate, Oslo, Norway
Natural History Museum, University of Oslo, Oslo, Norway
Cold Regions Research Centre, Wilfrid Laurier University, Waterloo, ON, Canada
Institute of Biophysics, Siberian Branch of Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Department of Ecology and Environmental Science, Climate Impacts Research Centre, Umea University, Abisko, Sweden
Paleoecological Environmental Assessment and Research Laboratory (PEARL), Department of Biology, Queen’s University, Kingston, ON, Canada
Norwegian Institute for Nature Research, Oslo, Norway
Canadian Rivers Institute and Department of Biology, University of New Brunswick, Fredericton, NB, Canada

Доп.точки доступа:
Huser, B. J.; Futter, M. N.; Bogan, D.; Brittain, J. E.; Culp, J. M.; Goedkoop, W.; Gribovskaya, I.; Karlsson, J.; Lau, D. C.P.; Ruhland, K. M.; Schartau, A. K.; Shaftel, R.; Smol, J. P.; Vrede, T.; Lento, J.

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16.

Spatial and temporal variation in Arctic freshwater chemistry-Reflecting climate-induced landscape alterations and a changing template for biodiversity / B. J. Huser, M. N. Futter, D. Bogan [et al.] // Freshw. Biol. - 2020, DOI 10.1111/fwb.13645. - Cited References:98. - Environment and Climate Change Canada; Cumulative Impact Monitoring Program, Government of Northwest Territories . - Article in press. - ISSN 0046-5070. - ISSN 1365-2427

РУБ Ecology + Marine & Freshwater Biology
Рубрики:
DISSOLVED ORGANIC-CARBON
PERMAFROST THAW
CHEMICAL LIMNOLOGY
Кл.слова (ненормированные):
biogeochemistry -- eutrophication -- lakes -- oligotrophication -- rivers
Аннотация: Freshwater chemistry across the circumpolar region was characterised using a pan-Arctic data set from 1,032 lake and 482 river stations. Temporal trends were estimated for Early (1970-1985), Middle (1986-2000), and Late (2001-2015) periods. Spatial patterns were assessed using data collected since 2001. Alkalinity, pH, conductivity, sulfate, chloride, sodium, calcium, and magnesium (major ions) were generally higher in the northern-most Arctic regions than in the Near Arctic (southern-most) region. In particular, spatial patterns in pH, alkalinity, calcium, and magnesium appeared to reflect underlying geology, with more alkaline waters in the High Arctic and Sub Arctic, where sedimentary bedrock dominated. Carbon and nutrients displayed latitudinal trends, with lower levels of dissolved organic carbon (DOC), total nitrogen, and (to a lesser extent) total phosphorus (TP) in the High and Low Arctic than at lower latitudes. Significantly higher nutrient levels were observed in systems impacted by permafrost thaw slumps. Bulk temporal trends indicated that TP was higher during the Late period in the High Arctic, whereas it was lower in the Near Arctic. In contrast, DOC and total nitrogen were both lower during the Late period in the High Arctic sites. Major ion concentrations were higher in the Near, Sub, and Low Arctic during the Late period, but the opposite bulk trend was found in the High Arctic. Significant pan-Arctic temporal trends were detected for all variables, with the most prevalent being negative TP trends in the Near and Sub Arctic, and positive trends in the High and Low Arctic (mean trends ranged from +0.57%/year in the High/Low Arctic to -2.2%/year in the Near Arctic), indicating widespread nutrient enrichment at higher latitudes and oligotrophication at lower latitudes. The divergent P trends across regions may be explained by changes in deposition and climate, causing decreased catchment transport of P in the south (e.g. increased soil binding and trapping in terrestrial vegetation) and increased P availability in the north (deepening of the active layer of the permafrost and soil/sediment sloughing). Other changes in concentrations of major ions and DOC were consistent with projected effects of ongoing climate change. Given the ongoing warming across the Arctic, these region-specific changes are likely to have even greater effects on Arctic water quality, biota, ecosystem function and services, and human well-being in the future.

WOS
Держатели документа:
Swedish Univ Agr Sci, Dept Aquat Sci & Assessment, Box 7050, S-75007 Uppsala, Sweden.
Univ Alaska Anchorage, Alaska Ctr Conservat Sci, Anchorage, AK USA.
Norwegian Water Resources & Energy Directorate, Oslo, Norway.
Univ Oslo, Nat Hist Museum, Oslo, Norway.
Wilfrid Laurier Univ, Cold Regions Res Ctr, Waterloo, ON, Canada.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia.
Umea Univ, Climate Impacts Res Ctr, Dept Ecol & Environm Sci, Umea, Sweden.
Queens Univ, Dept Biol, Paleoecol Environm Assessment & Res Lab PEARL, Kingston, ON, Canada.
Norwegian Inst Nat Res, Oslo, Norway.
Univ New Brunswick, Canadian Rivers Inst, Fredericton, NB, Canada.
Univ New Brunswick, Dept Biol, Fredericton, NB, Canada.

Доп.точки доступа:
Huser, Brian J.; Futter, Martyn N.; Bogan, Daniel; Brittain, John E.; Culp, Joseph M.; Goedkoop, Willem; Gribovskaya, Iliada; Karlsson, Jan; Lau, Danny C. P.; Ruhland, Kathleen M.; Schartau, Ann Kristin; Shaftel, Rebecca; Smol, John P.; Vrede, Tobias; Lento, Jennifer; Environment and Climate Change Canada; Cumulative Impact Monitoring Program, Government of Northwest Territories

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17.

SEQUENCE OF THE CDNA-ENCODING THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA [Text] / B. A. ILLARIONOV [et al.] // Gene. - 1995. - Vol. 153, Is. 2. - P273-274, DOI 10.1016/0378-1119(94)00797-V. - Cited References: 6 . - 2. - ISSN 0378-1119

РУБ Genetics & Heredity
Рубрики:
CA-2+-ACTIVATED PHOTOPROTEIN
AEQUORIN
CLONING
Кл.слова (ненормированные):
BIOLUMINESCENCE -- CALCIUM -- GENE -- PLASMID -- MARINE COELENTERATES
Аннотация: A cDNA clone encoding the Ca2+-activated photoprotein, obelin (Obl), from Obelia longissima was sequenced. The nucleotide (nt) sequence contained two long overlapping open reading frames (ORFs), one of which encoded apoobelin (apoObl). The deduced amino acid (aa) sequence of apoObl revealed that this 195-aa protein has three EF-hand structures that are characteristic for Ca2+-binding domains. Strong aa homology was shown among apoObl, apoaequorin and apoclytin. The second ORF present in the obl cDNA consists of 139 codons and encodes a very basic protein with a calculated pI of 10.56 and a molecular mass of 16153 Da.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
ILLARIONOV, B.A.; BONDAR, V.S.; ILLARIONOVA, V.A.; VYSOTSKI, E.S.

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18.

Semisynthetic photoprotein reporters for tracking fast Ca2+ transients / N. P. Malikova, A. J. Borgdorff, E. S. Vysotski // Photochem. Photobiol. Sci. - 2015. - Vol. 14, Is. 12. - P2213-2224, DOI 10.1039/c5pp00328h . - ISSN 1474-905X
Аннотация: Changes in the intracellular concentration of free ionized calcium ([Ca2+]i) control a host of cellular processes as varied as vision, muscle contraction, neuronal signal transmission, proliferation, apoptosis etc. The disturbance in Ca2+-signaling causes many severe diseases. To understand the mechanisms underlying the control by calcium and how disorder of this regulation relates to pathological conditions, it is necessary to measure [Ca2+]i. The Ca2+-regulated photoproteins which are responsible for bioluminescence of marine coelenterates have been successfully used for this purpose over the years. Here we report the results on comparative characterization of bioluminescence properties of aequorin from Aequorea Victoria, obelin from Obelia longissima, and clytin from Clytia gregaria charged by native coelenterazine and coelenterazine analogues f, i, and hcp. The comparison of specific bioluminescence activity, stability, emission spectra, stopped-flow kinetics, sensitivity to calcium, and effect of physiological concentrations of Mg2+ establishes obelin-hcp as an excellent semisynthetic photoprotein to keep track of fast intracellular Ca2+ transients. The rate of rise of its light signal on a sudden change of [Ca2+] is almost 3- and 11-fold higher than those of obelin and aequorin with native coelenterazine, respectively, and 20 times higher than that of the corresponding aequorin-hcp. In addition, obelin-hcp preserves a high specific bioluminescence activity and displays higher Ca2+-sensitivity as compared to obelin charged by native coelenterazine and sensitivity to Ca2+ comparable with those of aequorin-f and aequorin-hcp. © The Royal Society of Chemistry and Owner Societies 2015.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Institut des Neurosciences Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique, Avenue de la Terrasse, Gif-sur-Yvette, France

Доп.точки доступа:
Malikova, N. P.; Borgdorff, A. J.; Vysotski, E. S.
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19.

Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin / L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2016. - Vol. 15, Is. 5. - P691-704, DOI 10.1039/c6pp00050a . - ISSN 1474-905X
Аннотация: Bright bioluminescence of ctenophores is caused by Ca2+-regulated photoproteins. Although these photoproteins are functionally identical to and share many properties of cnidarian photoproteins, like aequorin and obelin, and retain the same spatial architecture, they are extremely sensitive to light, i.e. lose the ability to bioluminesce on exposure to light over the entire absorption spectrum. In addition, the degree of identity of their amino acid sequences with those of cnidarian photoproteins is only 29.4%. This suggests that the residues involved in bioluminescence of ctenophore and cnidarian photoproteins significantly differ. Here we describe the bioluminescent properties of berovin mutants with substitution of the residues located in the photoprotein internal cavity. Since the spatial structure of berovin bound with a substrate is not determined yet, to identify these residues we have modeled it with an accommodated substrate using the structures of some cnidarian Ca2+-regulated photoproteins with bound coelenterazine or coelenteramide as templates in order to obtain an adequate sampling and to take into account all possible conformers and variants for ligand-protein docking. Based on the impact of substitutions on the bioluminescent properties and model structures we speculate that within the internal cavity of ctenophore photoproteins, coelenterazine is bound as a 2-peroxy anion adduct which is stabilized owing to Coulomb interaction with a positively charged guanidinium group of Arg41 paired with Tyr204. In this case, the bioluminescence reaction is triggered by only calcium-induced conformational changes leading to the disturbance of charge-charge interaction. © 2016 The Royal Society of Chemistry and Owner Societies.

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

Доп.точки доступа:
Burakova, L. P.; Stepanyuk, G. A.; Eremeeva, E. V.; Vysotski, E. S.

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20.

Removal of essential ligand in N-terminal calcium binding domain of obelin does not inactivate the photoprotein or reduce its calcium sensitivity, but dramatically alters the kinetics of the luminescent reaction [Text] / V. A. Illarionova [et al.] ; ed.: JW Hastings, LJ Kricka, J Kricka, // BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS : JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - P431-434. - Cited References: 0 . - 4. - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Illarionova, V.A.; Illarionov, B.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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