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Untangling metabolic and spatial interactions of stress tolerance in plants. 1. Patterns of carbon metabolism within leaves / K. Y. Biel [et al.] // Protoplasma. - 2010. - Vol. 245, Is. 1. - P49-73, DOI 10.1007/s00709-010-0135-7 . - ISSN 0033-183X
Кл.слова (ненормированные):
Carbon metabolism -- Leaf anatomy -- Leaf form and function -- Maximal ecological utility -- Photosynthesis -- Stress tolerance Spinacia oleracea -- aspartate aminotransferase isoenzyme 1 -- bicarbonate -- carbon -- carbon dioxide -- catalase -- chlorophyll -- malate dehydrogenase -- oxygen -- ribulosebisphosphate carboxylase -- vegetable protein -- article -- enzymology -- histology -- light -- metabolism -- oxidation reduction reaction -- photosynthesis -- physiological stress -- physiology -- plant leaf -- spinach -- theoretical model -- Aspartate Aminotransferase, Cytoplasmic -- Bicarbonates -- Carbon -- Carbon Dioxide -- Catalase -- Chlorophyll -- Light -- Malate Dehydrogenase -- Models, Theoretical -- Oxidation-Reduction -- Oxygen -- Photosynthesis -- Plant Leaves -- Plant Proteins -- Ribulose-Bisphosphate Carboxylase -- Spinacia oleracea -- Stress, Physiological -- Spinacia oleracea
Аннотация: The localization of the key photoreductive and oxidative processes and some stress-protective reactions within leaves of mesophytic C3 plants were investigated. The role of light in determining the profile of Rubisco, glutamate oxaloacetate transaminase, catalase, fumarase, and cytochrome-c-oxidase across spinach leaves was examined by exposing leaves to illumination on either the adaxial or abaxial leaf surfaces. Oxygen evolution in fresh paradermal leaf sections and CO2 gas exchange in whole leaves under adaxial or abaxial illumination was also examined. The results showed that the palisade mesophyll is responsible for the midday depression of photosynthesis in spinach leaves. The photosynthetic apparatus was more sensitive to the light environment than the respiratory apparatus. Additionally, examination of the paradermal leaf sections by optical microscopy allowed us to describe two new types of parenchyma in spinach-pirum mesophyll and pillow spongy mesophyll. A hypothesis that oxaloacetate may protect the upper leaf tissue from the destructive influence of active oxygen is presented. The application of mathematical modeling shows that the pattern of enzymatic distribution across leaves abides by the principle of maximal ecological utility. Light regulation of carbon metabolism across leaves is discussed. В© 2010 Springer-Verlag.

Scopus
Держатели документа:
Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russian Federation
Biosphere Systems International Foundation, Oro Valley, AZ 85755, United States
International Scientific Centre for Organism Extreme States Research, Krasnoyarsk Scientific Centre, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Forest, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Biocompatible Plant Research Institute, College of Natural Sciences, California State University, Chico, CA 95929-0555, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Biel, K.Y.; Fomina, I.R.; Nazarova, G.N.; Soukhovolsky, V.G.; Khlebopros, R.G.; Nishio, J.N.

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

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

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

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

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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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Preferential oxidative dehalogenation upon conversion of 2-halophenols by Rhodococcus opacus 1G [Text] / V. S. Bondar [et al.] // FEMS Microbiol. Lett. - 1999. - Vol. 181, Is. 1. - P73-82, DOI 10.1111/j.1574-6968.1999.tb08828.x. - Cited References: 30 . - ISSN 0378-1097

РУБ Microbiology
Рубрики:
PHENOL HYDROXYLASE
   POLYCHLORINATED PHENOLS
   MICROBIAL-DEGRADATION
   TRICHOSPORON-CUTANEUM
   METABOLISM
   PURIFICATION
   REGIOSELECTIVITY
   CHLOROAROMATICS
   COMPONENT
   BENZOATE
Кл.слова (ненормированные):
phenol hydroxylase -- oxidative dehalogenation -- 2-halophenol -- F-19 NMR -- Rhodococcus opacus
Аннотация: The regiospecificity of hydroxylation of C2-halogenated phenols by Rhodococcus opacus 1G was investigated. Oxidative defluorination at the C2 position ortho with respect to the hydroxyl moiety was preferred over hydroxylation at the non fluorinated C6 position for all 2-fluorophenol compounds studied. Initial hydroxylation of 2,3,5-trichlorophenol resulted in the exclusive formation of 3,5-dichlorocatechol. These results indicate that, in contrast to all other phenol ortho-hydroxylases studied so far, phenol hydroxylase from R. opacus 1G is capable of catalyzing preferential oxidative defluorination but also oxidative dechlorination. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

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

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

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

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

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

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

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Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins / P. V. Natashin [et al.] // FEBS J. - 2014. - Vol. 281, Is. 5. - P1432-1445, DOI 10.1111/febs.12715 . - ISSN 1742-4658
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine, obelin -- 6 (4 hydroxyphenyl) derivative -- aequorin -- benzene derivative -- calcium ion -- hydromedusan -- mutant protein -- obelin -- oxygen -- photoprotein -- unclassified drug -- amino acid substitution -- article -- bioluminescence -- calcium transport -- crystal structure -- fluorescence -- hydrogen bond -- priority journal -- protein conformation -- protein structure -- wild type -- Coelenterata -- aequorin -- bioluminescence -- Ca2+-regulated photoprotein -- coelenterazine, obelin -- Amino Acid Substitution -- Animals -- Conserved Sequence -- Crystallography, X-Ray -- Hydrogen Bonding -- Hydrozoa -- Luminescent Proteins -- Models, Molecular -- Mutagenesis, Site-Directed -- Mutant Proteins -- Protein Conformation -- Spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.

Scopus
Держатели документа:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk 660036, Russian Federation
Laboratory of Bioluminescence Biotechnology, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Russian Federation
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States
IHuman Institute, ShanghaiTech University, Shanghai, China : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Markova, S.V.; Lee, J.; Vysotski, E.S.; Liu, Z.-J.

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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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Bioluminescent analysis of intensity of pathological oxidative processes in cells of perfused rat liver after hyperthermia / N. N. Remmel [et al.] // Bulletin of Experimental Biology and Medicine. - 2003. - Vol. 135, Is. 1. - P. 43-45, DOI 10.1023/A:1023489727703 . - ISSN 0007-4888
Кл.слова (ненормированные):
Bioluminescent analysis -- Controlled perfusion of isolated liver -- Hyperthermia oxidative stress -- thiobarbituric acid reactive substance -- animal experiment -- animal model -- animal tissue -- article -- bioluminescence -- concentration (parameters) -- controlled study -- correlation analysis -- female -- hyperthermia -- in vivo study -- lipid peroxidation -- liver metabolism -- liver perfusion -- male -- nonhuman -- oxidative stress -- oxygen consumption -- pathology -- rat -- thermal exposure -- Animals -- Female -- Hepatocytes -- Hyperthermia, Induced -- Liver -- Luminescent Measurements -- Male -- Oxidative Stress -- Perfusion -- Rats -- Animalia
Аннотация: We studied the possibility of evaluation of the intensity of pathological oxidative processes in rat liver using an integral bioluminescent test with controlled perfusion of the isolated organ. The test revealed a significant correlation between the level of TBA-reactive products and bioluminescence intensity.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Novosibirsk, Russian Federation
Krasnoyarsk State University, Krasnoyarsk, Russian Federation
Intl. Res. Ctr. of Extreme States, Siberian Division, Russian Academy of Sciences, Novosibirsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Remmel, N.N.; Kratasyuk, V.A.; Maznyak, O.M.; Inzhevatkin, E.V.; Nefedov, V.P.

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10.

Oxidative stress monitoring in biological samples by bioluminescent method / N. N. Remmel, N. M. Titova, V. A. Kratasyuk // Bulletin of Experimental Biology and Medicine. - 2003. - Vol. 136, Is. 2. - P. 209-211, DOI 10.1023/A:1026347830283 . - ISSN 0007-4888
Кл.слова (ненормированные):
Bioluminescent analysis -- Lipid peroxidation -- Malonic dialdehyde -- Oxidative stress -- malonaldehyde -- animal tissue -- article -- bioluminescence -- brain tissue -- controlled study -- fluorescence -- freeze drying -- kidney parenchyma -- lipid peroxidation -- liver -- male -- monitoring -- nonhuman -- oxidative stress -- Photobacterium phosphoreum -- rat -- serum -- Animals -- Bacteria -- Biological Assay -- Lipid Peroxidation -- Luminescent Measurements -- Malondialdehyde -- Oxidative Stress -- Photobacterium -- Rats -- Tissue Extracts -- Animalia -- Negibacteria -- Photobacterium -- Photobacterium phosphoreum
Аннотация: The integral bioluminescent biotest with lyophilized fluorescent bacteria was used for monitoring of LPO processes in tissue extracts and serum of rats exposed to stress. A relationship between the content of MDA (LPO indicator) and fluorescence of bacteria was observed in all biological samples.

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

Доп.точки доступа:
Remmel, N.N.; Titova, N.M.; Kratasyuk, V.A.

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11.

CHEMI-LUMINESCENT MEASUREMENTS OF THE NEUTROPHIL OXIDATIVE ACTIVITY DURING PHAGOCYTOSIS [Текст] / R. A. PAVLENKO, Y. A. KUDENKO // LABORATORNOE DELO. - 1988. - Is. 1. - P. 35-37. - Cited References: 0 . - ISSN 0023-6748

РУБ Medicine, General & Internal

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PAVLENKO, R.A.; KUDENKO, Y.A.

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12.

Oxidative stress monitoring in biological samples by bioluminescent method [Text] / N. N. Remmel', N. M. Titova, V. A. Kratasyuk // Bull. Exp. Biol. Med. - 2003. - Vol. 136, Is. 2. - P. 209-211, DOI 10.1023/A:1026347830283. - Cited References: 11 . - ISSN 0007-4888

РУБ Medicine, Research & Experimental

Кл.слова (ненормированные):
bioluminescent analysis -- oxidative stress -- lipid peroxidation -- malonic dialdehyde
Аннотация: The integral bioluminescent biotest with lyophilized fluorescent bacteria was used for monitoring of LPO processes in tissue extracts and serum of rats exposed to stress. A relationship between the content of MDA (LPO indicator) and fluorescence of bacteria was observed in all biological samples.

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

Доп.точки доступа:
Remmel', N.N.; Titova, N.M.; Kratasyuk, V.A.

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13.

Bioluminescent analysis of intensity of pathological oxidative processes in cells of perfused rat liver after hyperthermia [Text] / N. N. Remmel [et al.] // Bull. Exp. Biol. Med. - 2003. - Vol. 135, Is. 1. - P. 43-45, DOI 10.1023/A:1023489727703. - Cited References: 15 . - ISSN 0007-4888

РУБ Medicine, Research & Experimental

Кл.слова (ненормированные):
bioluminescent analysis -- controlled perfusion of isolated liver -- hyperthermia -- oxidative stress
Аннотация: We studied the possibility of evaluation of the intensity of pathological oxidative processes in rat liver using an integral bioluminescent test with controlled perfusion of the isolated organ. The test revealed a significant correlation between the level of TBA-reactive products and bioluminescence intensity.

WOS
Держатели документа:
Russian Acad Sci, Siberian Div, Inst Biophys, Moscow 117901, Russia
Krasnoyarsk State Univ, Krasnoyarsk, Russia
Russian Acad Sci, Siberian Div, Presidium Krasnoyarsk Res Ctr, Int Res Ctr Extreme States, Moscow 117901, Russia
ИБФ СО РАН
МНЦ КНЦ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Remmel, N.N.; Kratasyuk, V.A.; Maznyak, O.M.; Inzhevatkin, E.V.; Nefedov, V.P.

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14.

Pollutant toxicity and detoxification by humic substances: mechanisms and quantitative assessment via luminescent biomonitoring [Text] / N. S. Kudryasheva, A. S. Tarasova // Environ. Sci. Pollut. Res. - 2015. - Vol. 22, Is. 1. - P155-167, DOI 10.1007/s11356-014-3459-6. - Cited References:120. - The work was supported by the Russian Foundation for Basic Research,Grant No. 13-04-98072-sibir-a. Part of the work (analysis ofdetoxification of radioactive solutions) was supported by the RussianScience Foundation, Grant No. 14-14-00076. . - ISSN 0944-1344. - ISSN 1614-7499

РУБ Environmental Sciences
Рубрики:
PHOTOBACTERIUM-LEIOGNATHI LUCIFERASE
DISSOLVED ORGANIC-MATTER
Кл.слова (ненормированные):
Detoxification mechanisms -- Humic substances -- Pollutants -- Bioassays -- Bioluminescence
Аннотация: The paper considers mechanisms of detoxification of pollutant solutions by water-soluble humic substances (HSs), natural detoxifying agents. The problems and perspectives of bioassay application for toxicity monitoring of complex solutions are discussed from ecological point of view. Bioluminescence assays based on marine bacteria and their enzymes are of special attention here; they were shown to be convenient tools to study the detoxifying effects on cellular and biochemical levels. The advantages of bioluminescent enzymatic assay for monitoring both integral and oxidative toxicities in complex solutions of model pollutants and HS were demonstrated. The efficiencies of detoxification of the solutions of organic oxidizers and salts of metals (including radioactive ones) by HS were analyzed. The dependencies of detoxification efficiency on time of exposure to HS and HS concentrations were demonstrated. Antioxidant properties of HS were considered in detail. The detoxifying effects of HS were shown to be complex and regarded as 'external' (binding and redox processes in solutions outside the organisms) and/or 'internal' organismal processes. The paper demonstrates that the HS can stimulate a protective response of bacterial cells as a result of (1) changes of rates of biochemical reactions and (2) stabilization of mucous layers outside the cell walls. Acceleration of auto-oxidation of NADH, endogenous reducer, by HS was suggested as a reason for toxicity increase in the presence of HS due to abatement of reduction ability of intracellular media.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
RAS, Inst Biophys, SB, Krasnoyarsk 660036, Russia.
ИБФ СО РАН

Доп.точки доступа:
Kudryasheva, N.S.; Tarasova, A.S.; Russian Foundation for Basic Research [13-04-98072-sibir-a]; RussianScience Foundation [14-14-00076]

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15.

Antioxidant activity of humic substances via bioluminescent monitoring in vitro [Text] / A. S. Tarasova, D. I. Stom, N. S. Kudryasheva // Environ. Monit. Assess. - 2015. - Vol. 187, Is. 3. - Ст. 89, DOI 10.1007/s10661-015-4304-1. - Cited References:51. - This work was supported by the Russian Foundation for Basic Research, Grant No. 15-03-06786a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. . - ISSN 0167-6369. - ISSN 1573-2959

РУБ Environmental Sciences
Рубрики:
DETOXIFICATION PROCESSES
   TOXICITY
   BIOASSAYS
   BACTERIA
   ASSAY
Кл.слова (ненормированные):
Antioxidant activity -- Oxidative toxicity -- General toxicity -- Humic -- substances -- Bioassay -- Bioluminescence
Аннотация: This work considers antioxidant properties of natural detoxifying agents-humic substances (HS) in solutions of model inorganic and organic compounds of oxidative nature-complex salt K-3[Fe(CN)(6)] and 1,4-benzoquinone. Bioluminescent system of coupled enzymatic reactions catalyzed by NAD(P) H:FMN-oxidoreductase and bacterial luciferase was used as a bioassay in vitro to monitor toxicity of the oxidizer solutions. Toxicities of general and oxidative types were evaluated using bioluminescent kinetic parameters-bioluminescence intensity and induction period, respectively. Antioxidant activity of HS was attributed to their ability to decrease both general and oxidative toxicities; the HS antioxidant efficiency was characterized with detoxification coefficients D-GT and D-OxT, respectively. Dependencies of D-GT and D-OxT on HS concentration and time of preliminary incubation of the oxidizers with HS were demonstrated. The optimal conditions for detoxification of the oxidizers were >20-min incubation time and 0.5x10(-4) to 2x10(-4) M of HS concentration. The present study promotes application of the enzymatic luminescent bioassay to monitor toxicity of pollutants of oxidative nature in environmental and waste waters in remediation procedures.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Irkutsk State Univ, Irkutsk 664003, Russia.
ИБФ СО РАН

Доп.точки доступа:
Tarasova, A.S.; Stom, D.I.; Kudryasheva, N.S.; Russian Foundation for Basic Research [15-03-06786a]; Russian Academy of Sciences [VI 57.1.1]

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16.

Novel Mechanism of Bioluminescence: Oxidative Decarboxylation of a Moiety Adjacent to the Light Emitter of Fridericia Luciferin [Text] / M. A. Dubinnyi [et al.] // Angew. Chem.-Int. Edit. - 2015. - Vol. 54, Is. 24. - P7065-7067, DOI 10.1002/anie.201501668. - Cited References:15. - We thank Dr. K.V. Antonov for acquisition of LC-HRMS spectra and Prof. Gary Schuster for fruitful discussion. This work was supported by the Russian Science Foundation grant 14-50-00131. M.S.B. acknowledges support by a stipend program of the President of the Russian Federation. K.M.S. acknowledges generous support from the National Science Foundation (CHE-1213047). This research was carried out using the equipment provided by IBCH core facility (CKP IBCH). . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
CHEMILUMINESCENCE
CYPRIDINA
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- luciferin -- oxidative -- decarboxylation -- peptides
Аннотация: A novel luciferin from a bioluminescent Siberian earthworm Fridericia heliota was recently described. In this study, the Fridericia oxyluciferin was isolated and its structure elucidated. The results provide insight into a novel bioluminescence mechanism in nature. Oxidative decarboxylation of a lysine fragment of the luciferin supplies energy for light generation, while a fluorescent CompX moiety remains intact and serves as the light emitter.

WOS
Держатели документа:
Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.
Russian Acad Sci, Akademgorodok, Siberian Branch, Lab Photobiol,Inst Biophys, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Branch Shemyakin, Pushchino 142290, Russia.
Russian Acad Sci, Ovchinnikov Inst Bioorgan Chem, Pushchino 142290, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Baranov, Mikhail S.; Gorokhovatsky, Andrey Yu.; Kotlobay, Alexey; Solntsev, Kyril M.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]; President of the Russian Federation; National Science Foundation [CHE-1213047]

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17.

Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2015. - Vol. 51, Is. 4. - P419-424, DOI 10.1134/S0003683815040110. - Cited References:35. - The authors are grateful to N. V. Psurtseva (curator of the collection of basidiomycetes of the Botanical Institute, Russian Academy of Science) for help with the species affiliation of the IBSO 2328 culture. This work was supported by the Program of Interdisciplinary Projects of the Siberian Branch of the Russian Academy of Sciences, project no. 71. . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
OXIDATIVE STRESS
   SYSTEM
   FUNGI
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
basidiomycetes -- luminescence -- peroxidase -- catalase
Аннотация: The peroxidase and catalase activities in the mycelium of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in normal conditions and under stress were compared. An increase in the luminescence level was observed under stress, as well as an increase in peroxidase and catalase activities. Moreover, the peroxidase activity in extracts of A. borealis mycelium was found to be almost one and a half orders of magnitude lower, and the catalase activity more than two orders of magnitude higher in comparison with the N. nambi mycelium. It can be suggested that the difference between the brightly luminescent and dimly luminescent mycelium of N. nambi is due to the content of (HO2)-O-2 or other peroxide compounds.

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Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogil'naya, O. A.; Ronzhin, N. O.; Medvedeva, S. E.; Bondar', V. S.; Siberian Branch of the Russian Academy of Sciences [71]

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18.

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

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

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

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19.

On mechanism of antioxidant effect of fullerenols / A. S. Sachkova [et al.] // Biochem. Biophys. Rep. - 2017. - Vol. 9. - P1-8, DOI 10.1016/j.bbrep.2016.10.011 . - ISSN 2405-5808
Кл.слова (ненормированные):
Antioxidant activity -- Bacterial enzymes -- Fullerenol -- Hormesis -- Luminous marine bacteria -- Ultralow concentrations
Аннотация: Fullerenols are nanosized water-soluble polyhydroxylated derivatives of fullerenes, specific allotropic form of carbon, bioactive compounds and perspective pharmaceutical agents. Antioxidant activity of fullerenols was studied in model solutions of organic and inorganic toxicants of oxidative type – 1,4-benzoquinone and potassium ferricyanide. Two fullerenol preparations were tested: С60О2–4(ОН)20–24 and mixture of two types of fullerenols С60О2–4(ОН)20–24+С70О2–4(ОН)20–24. Bacteria-based and enzyme-based bioluminescent assays were used to evaluate a decrease in cellular and biochemical toxicities, respectively. Additionally, the enzyme-based assay was used for the direct monitoring of efficiency of the oxidative enzymatic processes. The bacteria-based and enzyme-based assays showed similar peculiarities of the detoxification processes: (1) ultralow concentrations of fullerenols were active (ca 10–17–10?4 and 10–17–10? 5 g/L, respectively), (2) no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and (3) detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effect of highly diluted fullerenol solutions on bacterial cells was attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. Sequence analysis of 16S ribosomal RNA was carried out; it did not reveal mutations in bacterial DNA. The suggestion was made that hydrophobic membrane-dependent processes are involved to the detoxifying mechanism. Catalytic activity of fullerenol (10? 8 g/L) in NADH-dependent enzymatic reactions was demonstrated and supposed to contribute to adaptive bacterial response. © 2016 The Authors

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Держатели документа:
National Research Tomsk Polytechnic University, Tomsk, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, Russian Federation
SB RAS Genomics Core Facility, Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibirsk, Russian Federation

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Churilov, G. N.; Guseynov, O. A.; Bondar, A. A.; Dubinina, I. A.; Kudryasheva, N. S.

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20.

Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa / M. D. Larionova, S. V. Markova, E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P503-510, DOI 10.1111/php.12694. - Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.

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

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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