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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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All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

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Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
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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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Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine [Text] / Z. J. Liu [et al.] // Biochem. Biophys. Res. Commun. - 2003. - Vol. 311, Is. 2. - P433-439, DOI 10.1016/j.bbrc.2003.09.231. - Cited References: 29 . - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENT PROTEIN
   VIOLET BIOLUMINESCENCE
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   PURIFICATION
   REFINEMENT
   EXPRESSION
Кл.слова (ненормированные):
photoprotein -- bioluminescence -- atomic resolution -- EF-hand
Аннотация: The spatial structure of the Ca2+-regulated photoprotein obelin has been solved to resolution of 1.1 Angstrom. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73 Angstrom resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca2+, the electron densities of both oxygen atoms became equally intense. In addition, one Ca2+ was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms. (C) 2003 Elsevier Inc. All rights reserved.

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:
Liu, Z.J.; Vysotski, E.S.; Deng, L...; Lee, J...; Rose, J...; Wang, B.C.

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Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobio1.2017.07.021. - Cited References:54. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 03562016-0712 and 0356-2015-0103) and the RFBR grant 17-04-00764. . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
SEQUENCE-ANALYSIS
   APO-OBELIN
   INTRINSIC FLUORESCENCE
   COELENTERAZINE
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Coelenteramide -- Cysteine -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or p-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coil, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild -type aequorin. In contrast, Cys-free obelin retains only 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a "fast" component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 0.2 and 44.6 0.4 C for aequorin and Cys-free aequorin, and 49.1 0.1 and 28.8 0.3 C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield.

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Держатели документа:
RAS, Photobiol Lab, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,SB, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Academy of Sciences [03562016-0712, 0356-2015-0103]; RFBR [17-04-00764]

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Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobiol.2017.07.021 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenteramide -- Coelenterazine -- Cysteine -- Photoprotein -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or ?-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coli, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. In contrast, Cys-free obelin retains only ~ 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a “fast” component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 ± 0.2 and 44.6 ± 0.4 °C for aequorin and Cys-free aequorin, and 49.1 ± 0.1 and 28.8 ± 0.3 °C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield. © 2017 Elsevier B.V.

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

Доп.точки доступа:
Eremeeva, E. V.; Vysotski, E. S.

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Bioluminescent properties of obelin and aequorin with novel coelenterazine analogues [Text] / R. . Gealageas [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 11. - P2695-2707, DOI 10.1007/s00216-014-7656-4. - Cited References: 57. - R.G. acknowledges the ICSN for a fellowship. We are grateful for the ANR grant to P.B. and a CNRS Physics, Chemistry and Biology interface grant to R.H.D. and P.B.; N.P.M, L.P.B., and E.S.V. acknowledge the RFBR grant 12-04-00131 and the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant 11.G34.31.0058). P.B. and A.J.B. are indebted to Eric Karplus from Science Wares Inc. for helping with single-photon imaging software. . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
PHOTOPROTEIN OBELIN
   CRYSTAL-STRUCTURE
   CA2+-REGULATED PHOTOPROTEINS
   CA2+-ACTIVATED PHOTOPROTEIN
   SEMISYNTHETIC AEQUORINS
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   BINDING PROTEIN
   CALCIUM-BINDING
   CA2+ DYNAMICS
Кл.слова (ненормированные):
Bioluminescence -- Luciferase -- Photoprotein -- Coelenterazine
Аннотация: The main analytical use of Ca2+-regulated photoproteins from luminous coelenterates is for real-time non-invasive visualization of intracellular calcium concentration ([Ca2+](i)) dynamics in cells and whole organisms. A limitation of this approach for in vivo deep tissue imaging is the fact that blue light emitted by the photoprotein is highly absorbed by tissue. Seven novel coelenterazine analogues were synthesized and their effects on the bioluminescent properties of recombinant obelin from Obelia longissima and aequorin from Aequorea victoria were evaluated. Only analogues having electron-donating groups (m-OCH3 and m-OH) on the C6 phenol moiety or an extended resonance system at the C8 position (1-naphthyl and alpha-styryl analogues) showed a significant red shift of light emission. Of these, only the alpha-styryl analogue displayed a sufficiently high light intensity to allow eventual tissue penetration. The possible suitability of this compound for in vivo assays was corroborated by studies with aequorin which allowed the monitoring of [Ca2+](i) dynamics in cultured CHO cells and in hippocampal brain slices. Thus, the alpha-styryl coelenterazine analogue might be potentially useful for non-invasive, in vivo bioluminescence imaging in deep tissues of small animals.

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Держатели документа:
[Gealageas, Ronan
Dodd, Robert H.] Ctr Natl Rech Sci, Inst Chim Subst Nat, UPR 2301, F-91198 Gif Sur Yvette, France
[Malikova, Natalia P.
Burakova, Ludmila P.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Malikova, Natalia P.
Burakova, Ludmila P.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Picaud, Sandrine
Borgdorff, Aren J.
Brulet, Philippe] Ctr Natl Rech Sci, Inst Neurosci Alfred Fessard, UPR 3294, F-91198 Gif Sur Yvette, France
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gealageas, R...; Malikova, N.P.; Picaud, S...; Borgdorff, A.J.; Burakova, L.P.; Brulet, P...; Vysotski, E.S.; Dodd, R.H.; ICSN; CNRS Physics, Chemistry and Biology interface grant; RFBR [12-04-00131]; Government of Russian Federation [11.G34.31.0058]; ANR

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Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents / E. V. Eremeeva, T. Y. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446, DOI 10.3390/ijms21155446. - Cited References:50. - The reported study was funded by RFBR and NSFC according to the research project No. 20-54-53011 (E.V.E. and N.P.M.), Russian Foundation for Basic Research (No. 18-44-242001), Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science (E.S.V.), the National Natural Science Foundation of China (No. 81874308), and the Shandong Natural Science Foundation (No. ZR2018ZC0233) (M.L.). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
photoprotein -- obelin -- aequorin -- coelenterazine -- analogues
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Fed Res Ctr, Krasnoyarsk 660036, Russia.
Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Key Lab Chem Biol MOE, Jinan 250012, Peoples R China.
Shandong Univ, Helmholtz Inst Biotechnol, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China.

Доп.точки доступа:
Eremeeva, Elena, V; Jiang, Tianyu; Malikova, Natalia P.; Li, Minyong; Vysotski, Eugene S.; RFBRRussian Foundation for Basic Research (RFBR); NSFCNational Natural Science Foundation of China (NSFC) [20-54-53011]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-44-242001]; Krasnoyarsk Regional Fund of Science; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81874308]; Shandong Natural Science FoundationNatural Science Foundation of Shandong Province [ZR2018ZC0233]; Government of Krasnoyarsk Territory

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Bioluminescent properties of semi-synthetic obelin and aequorin activated by coelenterazine analogues with modifications of C-2, C-6, and C-8 substituents / E. V. Eremeeva, T. Jiang, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 15. - Ст. 5446. - P1-21, DOI 10.3390/ijms21155446 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Analogues -- Coelenterazine -- Obelin -- Photoprotein
Аннотация: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong 250012, China
State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao, Shandong 266237, China

Доп.точки доступа:
Eremeeva, E. V.; Jiang, T.; Malikova, N. P.; Li, M.; Vysotski, E. S.

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10.

Ca(2+)-activator of the luminescence system of the earthworms Henlea sp., (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar, V. N. Petushkov // Doklady. Biochemistry and biophysics. - 2002. - Vol. 386. - P260-263 . - ISSN 1607-6729
Кл.слова (ненормированные):
calcium -- divalent cation -- edetic acid -- luciferase -- luciferin -- metal -- animal -- annelid worm -- article -- chemistry -- dose response -- enzymology -- genetics -- kinetics -- luminescence -- metabolism -- Animals -- Calcium -- Cations, Divalent -- Dose-Response Relationship, Drug -- Edetic Acid -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Metals -- Oligochaeta

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

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

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11.

Ca2+-regulated photoproteins: Structural insight into the bioluminescence mechanism [Text] / E. S. Vysotski, J. . Lee // Accounts Chem. Res. - 2004. - Vol. 37, Is. 6. - P405-415, DOI 10.1021/ar0400037. - Cited References: 44 . - ISSN 0001-4842

РУБ Chemistry, Multidisciplinary
Рубрики:
AEQUORIN BIOLUMINESCENCE
   SEQUENCE-ANALYSIS
   CALCIUM-BINDING
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   FUNCTIONAL PART
   EXCITED-STATES
   W92F OBELIN
   COELENTERAZINE
Аннотация: The bioluminescent jellyfish has contributed two famous proteins to modern science: green fluorescent protein or GFP, which finds wide use as a probe in cell biology studies, and aequorin, which has been used for intracellular calcium measurement for more than 30 years. More recently, obelin, a protein from the bioluminescent hydroid and also in the family of what are called "Ca2+-regulated photoproteins", has been shown to have very attractive properties both in general applications and for basic structural biology investigations. This review will survey the new information into their molecular mechanism of bioluminescence action.

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

Доп.точки доступа:
Vysotski, E.S.; Lee, J...

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12.

Ca2+-triggered coelenterazine-binding protein from Renilla as an enzyme-dependent label for binding assay [Text] / V. V. Krasitskaya [et al.] // Anal. Bioanal. Chem. - 2011. - Vol. 401, Is. 8. - P2573-2579, DOI 10.1007/s00216-011-5343-2. - Cited References: 17. - The work was supported by a "Leading Scientific School" (N 64987.2010.4) grant from the President of the Russian Federation and the "Molecular and Cell Biology" Program from the RAS. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
BIOLUMINESCENT IMMUNOASSAY
   LUCIFERASE
   PURIFICATION
   RENIFORMIS
   MUELLERI
   OBELIN
   PHOTOPROTEIN
   EXPRESSION
   SUBSTRATE
   CLONING
Кл.слова (ненормированные):
Ca2+-triggered coelenterazine-binding protein (CBP) -- Renilla muelleri luciferase -- Bioluminescent solid-phase microassay
Аннотация: The recombinant Ca2+-triggered coelenterazine-binding protein (CBP) from Renilla muelleri was investigated as a biospecifically labeled molecule for in vitro assay applications. The protein was shown to be stable in solutions in the frozen state, as well as stable under heating and to chemical modifications. Conjugates with biotin, oligonucleotide, and proteins were obtained and applied as biospecific molecules in a solid-phase microassay. CBP detection was performed with intact (no modifications were made) Renilla luciferase in the presence of calcium, and the detection limit was found to be 75 amol. Model experiments indicate that this approach shows much promise, especially with regard to the development of multianalytical systems.

Держатели документа:
[Korneeva, S. I.
Kudryavtsev, A. N.
Frank, L. A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Krasitskaya, V. V.
Markova, S. V.
Stepanyuk, G. A.
Frank, L. A.] Russian Acad Sci SB, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Krasitskaya, V.V.; Korneeva, S.I.; Kudryavtsev, A.N.; Markova, S.V.; Stepanyuk, G.A.; Frank, L.A.

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13.

Calcium-regulated photoprotein obelin as a label in immunoassay: An outlook for applications [Text] / L. A. Frank, V. V. Borisova, E. . Vysotski ; ed. A Tsuji [et al.] // Bioluminescence & Chemiluminescence: Progress and Perspectives : WORLD SCIENTIFIC PUBL CO PTE LTD, 2005. - 13th International Symposium on Bioluminescence and Chemiluminescence (AUG 02-06, 2004, Yokohama, JAPAN). - P. 463-466, DOI 10.1142/9789812702203_0110. - Cited References: 7 . - ISBN 981-256-118-8

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Applied + Chemistry, Physical + Optics
Рубрики:
BIOLUMINESCENT IMMUNOASSAY

WOS
Держатели документа:
RAS, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Vysotski, E...; Tsuji, A \ed.\; Matsurnoto, M \ed.\; Maeda, M \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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14.

Calcium-regulated photoproteins of marine coelenterates [Text] / E. S. Vysotski, S. V. Markova, L. A. Frank // Mol. Biol. - 2006. - Vol. 40, Is. 3. - P355-367, DOI 10.1134/S0026893306030022. - Cited References: 99 . - ISSN 0026-8933

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINOMETRIC HYBRIDIZATION ASSAYS
   HYDROID OBELIA-GENICULATA
   GREEN-FLUORESCENT PROTEIN
   POLYMERASE-CHAIN-REACTION
   BIOLUMINESCENT IMMUNOASSAY
   RECOMBINANT AEQUORIN
   CRYSTAL-STRUCTURE
   BIOTINYLATED AEQUORIN
   ANGSTROM RESOLUTION
   CA2+-REGULATED PHOTOPROTEINS
Кл.слова (ненормированные):
bioluminescence -- obelin -- aequorin -- intracellular calcium -- molecular diagnosis
Аннотация: Calcium-regulated photoproteins are bioluminescent proteins that are responsible for the luminescence of marine coelenterates. A photoprotein molecule is a stable enzyme-substrate complex consisting of a single polypeptide chain and an oxygen-preactivated substrate, 2-hydroperoxcoelenterazine, which is tightly but noncovalently bound with the protein. Bioluminescence is triggered by Ca2+ and results from decarboxylation of the substrate bound with the protein. This review considers the current information about the structure of photoproteins, the mechanism of the bioluminescent reaction, the function of particular amino acid residues of the active center in catalysis and the formation of the emitter, and the use of photoproteins in bioluminescent microanalysis.

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

Доп.точки доступа:
Vysotski, E.S.; Markova, S.V.; Frank, L.A.

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15.

^a343.17.27.07.09.05^2VINITI
C36

Ca{2+}-активируемый фотопротеин обелин как индикатор кальциевого транспорта в протеолипосомах, включающих мембраны Т-системы скелетных мышц [Текст] : научное издание / В. С. Бондарь [и др.] // Биохимия. - 1991. - Т. 56, N 5. - С. 806-811 . - ISSN 0320-9725

ГРНТИ

34.17.27

РУБ 343.17.27.07.09.05
Рубрики:
ФОТОПРОТЕИНЫ
   КАЛЬЦИЙ-АКТИВИРУЕМЫЕ
   ОБЕЛИН
   ТРАНСПОРТ КАЛЬЦИЯ
   ПРОТЕОЛИПОСОМЫ
   МЕМБРАНЫ Т-СИСТЕМЫ СКЕЛЕТНЫХ МЫШЦ
   PHOTOPROTEIN
   CALCIUM TRANSPORT
   OBELIN
   PROTEOLIPOSOME
   MEMBRANE
Аннотация: В работе представлены данные о Ca{2+}-активируемом фотопротеине обелине как индикаторе кальциевого транспорта в протеолипосомах. Показано, что протеолипосомы, сформированные из лецитина и мембран T-системы скелетных мышц кролика, обладают проницаемостью к ионам кальция, активируемой 10{-5 }M BAY K-8644; 5*10{-5 }M нитендипин ингибирует действие BAY K-8644. Липосомы не проявляли чувствительности к исследуемым агентам. Ca{2+}-активируемый фотопротеин обелин является перспективным инструментом для изучения быстрых кальциевых потоков
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Высоцкий, Е.С.; Рожманова, О.М.; Воронина, С.Г.

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16.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration [Text] / N. P. Malikova [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5715-5726, DOI 10.1007/s00216-014-7986-2. - Cited References: 67. - This work was supported by RFBR grant 12-04-00131, 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 Russian Academy of Sciences, and the grant from the President of the Russian Federation "Leading Science School" (3951.2012.4). . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
   CTENOPHORE BEROE ABYSSICOLA
   GREEN-FLUORESCENT PROTEIN
   INTRACELLULAR CALCIUM
   SEQUENCE-ANALYSIS
   CA-2+-ACTIVATED PHOTOPROTEIN
   CA2+-BINDING PHOTOPROTEIN
   SEMISYNTHETIC AEQUORINS
   LUMINESCENT PROTEIN
   RECOMBINANT OBELIN
Кл.слова (ненормированные):
Calcium -- Coelenterazine -- Aequorin -- Obelin -- Clytin -- Mitrocomin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y(2) receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration.

WOS
Держатели документа:
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Burakova, L.P.; Markova, S.V.; Vysotski, E.S.; RFBR [12-04-00131]; Government of the Russian Federation [11.G34.31.0058]; Russian Academy of Sciences; Russian Federation "Leading Science School" [3951.2012.4]

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17.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca2+concentration / N. P. Malikova [et al.] // . - 2014, DOI 10.1007/s00216-014-7986-2 . - ISSN 1618-2642
Кл.слова (ненормированные):
Aequorin -- Calcium -- Clytin -- Coelenterazine -- Mitrocomin -- Obelin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y2 receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration. [Figure not available: see fulltext.] © 2014 Springer-Verlag Berlin Heidelberg.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, 660036, Russian Federation
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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18.

Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase [Text] / M. S. Titushin [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 2. - P189-196, DOI 10.1039/b713109g. - Cited References: 41 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
CRYSTAL-STRUCTURE
   LIGHT-EMISSION
   CA2+-REGULATED PHOTOPROTEINS
   BIOLUMINESCENT REPORTER
   RENIFORMIS LUCIFERASE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   ENERGY-TRANSFER
   EXCITED-STATE
   CALCIUM
Аннотация: The Renilla bioluminescent system in vivo is comprised of three proteins-the luciferase, green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called luciferin-binding protein (LBP). This work reports the cloning of the full-size cDNA encoding CBP from soft coral Renilla muelleri, its overexpression and properties of the recombinant protein. The apo-CBP was quantitatively converted to CBP by simple incubation with coelenterazine. The physicochemical properties of this recombinant CBP are determined to be practically the same as those reported for the CBP (LBP) of R. reniformis. CBP is a member of the four-EF-hand Ca2+-binding superfamily of proteins with only three of the EF-hand loops having the Ca2+-binding consensus sequences. There is weak sequence homology with the Ca2+-regulated photoproteins but only as a result of the necessary Ca2+-binding loop structure. In combination with Renilla luciferase, addition of only one Ca2+ is sufficient to release the coelenterazine as a substrate for the luciferase for bioluminescence. This combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone as the substrate for luciferase. This increased quantum yield, a difference of bioluminescence spectra, and markedly different kinetics, implicate that a CBP-luciferase complex might be involved.

Держатели документа:
[Titushin, Maxim S.
Markova, Svetlana V.
Frank, Ludmila A.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Lee, John
Vysotski, Eugene S.] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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19.

Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase [Text] / G. A. Stepanyuk [et al.] // Anal. Bioanal. Chem. - 2010. - Vol. 398, Is. 4. - P1809-1817, DOI 10.1007/s00216-010-4106-9. - Cited References: 39. - This work was supported by grant 09-04-12022 of the Russian Foundation for Basic Research, "Molecular and Cell Biology" program of Russian Academy of Sciences, by the SB RAS grant No. 2, and by the SB RAS Lavrentiev grant for Young Scientists. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
GREEN-FLUORESCENT PROTEIN
   BIOLUMINESCENT REPORTER
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   RECOMBINANT OBELIN
   GENE-EXPRESSION
   IN-VIVO
   CDNA
   CLONING
   PURIFICATION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Calcium -- Imaging
Аннотация: It has been shown that the coelenterazine analog, coelenterazine-v, is an efficient substrate for a reaction catalyzed by Renilla luciferase. The resulting bioluminescence emission maximum is shifted to a longer wavelength up to 40 nm, which allows the use of some "yellow" Renilla luciferase mutants for in vivo imaging. However, the utility of coelenterazine-v in small-animal imaging has been hampered by its instability in solution and in biological tissues. To overcome this drawback, we ligated coelenterazine-v to Ca2+-triggered coelenterazine-binding protein from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The coelenterazine-v bound within coelenterazine-binding protein has revealed a greater long-term stability at both 4 and 37 degrees C. In addition, the coelenterazine-binding protein ligated by coelenterazine-v yields twice the total light over free coelenterazine-v as a substrate for the red-shifted R. muelleri luciferase. These findings suggest the possibility for effective application of coelenterazine-v in various in vitro assays.

Держатели документа:
[Stepanyuk, Galina A.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Unch, James] Promega Biosci LLC, San Luis Obispo, CA 93401 USA
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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20.

Content of metals in compartments of ecosystem of a Siberian pond / M. I. Gladyshev [et al.] // Archives of Environmental Contamination and Toxicology. - 2001. - Vol. 41, Is. 2. - P157-162, DOI 10.1007/s002440010233 . - ISSN 0090-4341
Кл.слова (ненормированные):
aluminum -- cadmium -- calcium -- chromium -- copper -- heavy metal -- iron -- lead -- magnesium -- manganese -- nickel -- potassium -- sodium -- zinc -- aquatic ecosystem -- biological uptake -- heavy metal -- pond -- article -- bioaccumulation -- ecosystem -- fish -- nonhuman -- pond -- priority journal -- Russian Federation -- sediment -- soil pollution -- water contamination -- Animals -- Ecosystem -- Environmental Monitoring -- Fishes -- Geologic Sediments -- Invertebrates -- Metals, Heavy -- Plants -- Water Pollutants -- Russian Federation
Аннотация: During three field seasons (June-September) of 1997-99 contents of Na, K, Ca, Mg, Fe, Mn, Zn, Cu, Al, Cr, Ni, Cd, and Pb were determined in compartments of ecosystem (surrounding soils, bottom sediments, water, zoobenthos, macrophytes, and fish) of a fish and recreation pond situated at the edge of Krasnoyarsk City (Siberia, Russia). Contents of most parts of metals in soils, water, and macrophytes significantly correlated with each other. As concluded, their contents were determined by natural, general, geochemical peculiarities of the region. Heavy metals, contents of which were higher than federal upper limits of concentration, were revealed. In muscles of fish with different feeding spectra - crucian and perch - concentrations of some metals differed significantly; correlation graphs for metals also had different structures. Comparison of our data with those on diverse aquatic ecosystems of Siberia, Europe, North America, and China published in the last decade was carried out. It was concluded that a distribution of heavy metals in the compartments of an aquatic ecosystem presently have to be determined for each particular water body until general regularities are discovered.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation
Krasnoyarsk State University, Svobodny av., 79, Krasnoyarsk, 660042, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gladyshev, M.I.; Gribovskaya, I.V.; Moskvicheva, A.V.; Muchkina, E.Y.; Chuprov, S.M.; Ivanova, E.A.

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