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

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

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

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Effect of boiling and frying on the content of essential polyunsaturated fatty acids in muscle tissue of four fish species / M. I. Gladyshev [et al.] // Food Chemistry. - 2007. - Vol. 101, Is. 4. - P1694-1700, DOI 10.1016/j.foodchem.2006.04.029 . - ISSN 0308-8146
Кл.слова (ненормированные):
Cod -- Essential polyunsaturated fatty acids -- Herring -- Sole -- Trout -- docosahexaenoic acid -- icosapentaenoic acid -- polyunsaturated fatty acid -- article -- Atlantic cod -- Atlantic herring -- boiling point -- brown trout -- controlled study -- cooking -- fish -- food processing -- frying -- Lepidopsetta bilineata -- muscle tissue -- nonhuman -- Norway -- raw meat -- Russian Federation -- sample -- Clupea pallasi -- Clupeidae -- Gadus ogac -- Lepidopsetta bilineata -- Martes pennanti -- Paraplagusia bilineata -- Salmo trutta -- Salmonidae
Аннотация: Frozen samples of common fish species, sea trout (Salmo trutta), from Norway and Siberia, herring (Clupea harengus pallasi), rock sole (Lepidopsetta bilineata) and cod (Gadus morhua maris-albi), collected from a wholesale market in Krasnoyarsk city (Siberia, Russia) were analyzed. Special attention was paid to long-chain essential polyunsaturated fatty acids: eicosapentaenoic, 20:5?3 (EPA) and docosahexaenoic, 22:6?3 (DHA). Heat-treatment (cooking and frying) did not in general significantly decrease the contents of EPA and DHA compared to raw fish species, except for a modest reduction in Norwegian trout during frying. Boiled trout appeared to be a more valuable fish dish for obtaining the officially recommended appropriate daily intake of EPA + DHA for humans. Herring and sole had intermediate values, while boiled cod had a comparatively low value. В© 2006 Elsevier Ltd. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Krasnoyarsk State Trade-Economical Institute, Lidiya Prushinskaya Street, 2, Krasnoyarsk 660075, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gladyshev, M.I.; Sushchik, N.N.; Gubanenko, G.A.; Demirchieva, S.M.; Kalachova, G.S.

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Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2013. - Vol. 12, Is. 6. - P1016-1024, DOI 10.1039/c3pp00002h. - Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program. . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   CA2+-BINDING PHOTOPROTEIN
   SEQUENCE-ANALYSIS
   CRYSTAL-STRUCTURE
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   MNEMIOPSIS-LEIDYI
   LIGHT-EMISSION
   W92F OBELIN
   CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.

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Green-Fluorescent Protein from the Bioluminescent Jellyfish Clytia gregaria Is an Obligate Dimer and Does Not Form a Stable Complex with the Ca2+-Discharged Photoprotein Clytin [Text] / N. P. Malikova [et al.] // Biochemistry. - 2011. - Vol. 50, Is. 20. - P4232-4241, DOI 10.1021/bi101671p. - Cited References: 50. - This work was supported by NATO Collaborative Linkage Grant 979229, Grants SB RAS No. 2 and RFBR 08-04-92209, 09-04-12022, and 09-04-00172, the MCB program of the Russian Academy of Sciences, and Bayer AG. . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
VIBRIO-FISCHERI Y1
   ENERGY-TRANSFER
   CORRELATION SPECTROSCOPY
   BACTERIAL LUCIFERASE
   REFRACTIVE-INDEX
   PHOTOBACTERIUM-LEIOGNATHI
   POLARIZED FLUORESCENCE
   EXCITATION TRANSFER
   RECOMBINANT OBELIN
   LUMAZINE PROTEIN
Аннотация: Green-fluorescent protein (GFP) is the origin of the green bioluminescence color exhibited by several marine hydrozoans and anthozoans. The mechanism is believed to be Forster resonance energy transfer (FRET) within a luciferase GFP or photoprotein-GFP complex. As the effect is found in vitro at micromolar concentrations, for FRET to occur this complex must have an affinity in the micromolar range. We present here a fluorescence dynamics investigation of the recombinant bioluminescence proteins from the jellyfish Clytia gregaria, the photoprotein clytin in its Ca2+-discharged form that is highly fluorescent (lambda(max) = 506 nm) and its GFP (cgreGFP; lambda(max) = 500 nm). Ca2+-discharged clytin shows a predominant fluorescence lifetime of 5.7 ns, which is assigned to the final emitting state of the bioluminescence reaction product, coelenteramide anion, and a fluorescence anisotropy decay or rotational correlation time of 12 ns (20 degrees C), consistent with tight binding and rotation with the whole protein. A 34 ns correlation time combined with a translational diffusion constant and molecular brightness from fluorescence fluctuation spectroscopy all confirm that cgreGFP is an obligate dimer down to nanomolar concentrations. Within the dimer, the two chromophores have a coupled excited-state transition yielding fluorescence depolarization via FRET with a transfer correlation time of 0.5 ns. The 34 ns time of cgreGFP showed no change upon addition of a 1000-fold excess of Ca2+-discharged clytin, indicating no stable complexation below 0.2 mM. It is proposed that any bioluminescence FRET complex with micromolar affinity must be one formed transiently by the cgreGFP dimer with a short-lived (millisecond) intermediate in the clytin reaction pathway.

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Malikova, Natalia P.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
[Visser, Nina V.
van Hoek, Arie] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Nina V.
van Hoek, Arie
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Skakun, Victor V.] Belarusian State Univ, Dept Syst Anal, Minsk 220050, Byelarus
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Visser, N.V.; van Hoek, A...; Skakun, V.V.; Vysotski, E.S.; Lee, J...; Visser, AJWG

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Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 angstrom: Why it is not a calcium-regulated photoprotein [Text] / G. A. Stepanyuk [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 4. - P442-447, DOI 10.1039/b716535h. - Cited References: 49 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
HYDROID OBELIA-GENICULATA
   AMINO-ACID-SEQUENCE
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   ENERGY-TRANSFER
   CDNA CLONING
   BIOLUMINESCENCE
   AEQUORIN
   PURIFICATION
   EXPRESSION
Аннотация: Bioluminescence in the sea pansy Renilla involves two distinct proteins, a Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP contains one tightly bound coelenterazine molecule, which becomes available for reaction with luciferase and O-2 only subsequent to Ca2+ binding. CBP belongs to the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand" Ca2+-binding sites. The overall spatial structure of recombinant selenomethionine-labeled CBP determined at 1.7 angstrom, is found to approximate the protein scaffold characteristic of the class of Ca2+-regulated photoproteins. Photoproteins however, catalyze molecular oxygen addition to coelenterazine producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the bioluminescence reaction. However in CBP this first step of oxygen addition is not allowed. The different amino acid environments and hydrogen bond interactions within the binding cavity are proposed to account for the different properties of the two classes of proteins.

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

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

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THE MAIN FUNCTION OF HIS175, TRP179, AND TYR190 RESIDUES OF THE OBELIN BINDING SITE IS TO STABILIZE THE HYDROPEROXYCOELENTERAZINE INTERMEDIATE [Text] / E. V. Eremeeva [et al.] ; ed. AA Szalay [et al.] // BIOLUMINESCENCE AND CHEMILUMINESCENCE: CHEMISTRY, BIOLOGY AND APPLICATIONS : WORLD SCIENTIFIC PUBL CO PTE LTD, 2007. - 14th International Symposium on Bioluminescence and Chemiluminescence (OCT 15-19, 2006, San Diego, CA). - P7-10, DOI 10.1142/9789812770196_0002. - Cited References: 7 . - ISBN 978-981-270-816-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Applied
Рубрики:
PHOTOPROTEIN OBELIN
BIOLUMINESCENCE

Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Frank, L. A.
Vysotski, E. S.] Inst Biophys SB RAS, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Vysotski, E.S.; Szalay, AA \ed.\; Hill, PJ \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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The main function of His175, Trp179, and Tyr190 residues of the obelin-binding site is to stabilize the hydroperoxycoelenterazine intermediate [Text] / E. V. Eremeeva [et al.] // Luminescence. - 2006. - Vol. 21, Is. 5. - P275-276. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
RAS, SB, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Mol Biol & Biochem, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Lee, J...; Vysotski, E.S.

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AsLn2, a luciferin-related modified tripeptide from the bioluminescent earthworm Fridericia heliota / V. N. Petushkov [et al.] // Tetrahedron Letters. - 2014. - Vol. 55, Is. 2. - P463-465, DOI 10.1016/j.tetlet.2013.11.061 . - ISSN 0040-4039
Кл.слова (ненормированные):
Bioluminescence -- Fridericia heliota -- Luciferin -- Modified peptide
Аннотация: AsLn2, an unusual modified peptide, was isolated from the bioluminescent earthworm Fridericia heliota (Enchytraeidae). Its structure, elucidated by NMR and mass spectrometry, includes residues of tyrosine, CompX (a novel tyrosine modification product, reported in the accompanying paper), and N(omega)-acylated lysine. Chromatography, UV, and 1H NMR data imply a close structural similarity of AsLn2 with F. heliota luciferin. AsLn2 appears to be an intermediate or by-product in F. heliota luciferin biosynthesis. © 2013 Elsevier Ltd. All rights reserved.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi, 79, Krasnoyarsk 660041, Russian Federation
Laboratory of Photobiology, Institute of Biophysics, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation
Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, Campo Alegre St. 687, Porto 4169-007, Portugal
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Dubinnyi, M.A.; Rodionova, N.S.; Nadezhdin, K.D.; Marques, S.M.; Esteves Da Silva, J.C.G.; Shimomura, O.; Yampolsky, I.V.

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Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive [Text] / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931. - Cited References: 41 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
BACTERIAL LUCIFERASE
   LUMAZINE PROTEIN
   FLAVIN INTERMEDIATE
   ANGSTROM RESOLUTION
   RIBOFLAVIN PROTEIN
   PURIFICATION
   MECHANISM
   EMISSION
   ALDEHYDE
   INHIBITION
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects call be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, when the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on-off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme, These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found or the protein-protein interaction in the absence of the aliphatic component.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M...; Gibson, B.G.; Lee, J...

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10.

Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1 [Text] / V. N. Petushkov, B. G. Gibson, J. . Lee // Biochemistry. - 1996. - Vol. 35, Is. 25. - P8413-8418, DOI 10.1021/bi952691v. - Cited References: 24 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
LUMAZINE PROTEIN
   LUMINOUS BACTERIUM
   STRAIN Y-1
   BIOLUMINESCENCE
   EMISSION
   PURIFICATION
   TRANSIENT
   LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOLEC BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J...

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11.

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

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- temperature -- activation energy
Аннотация: Effects of temperature on bioluminescent patterns of luciferases from luminescent bacteria Vibrio harveyi, Vibrio fischeri, Photobacterium leiognathi, and Photobacterium phosphoreum were studied. The highest luminescence level was observed at 15-25 degrees C for the luciferase from P. phosphoreum, at 20-30 degrees C for the V. fischeri and P. leiognathi enzymes, and at 30-37 degrees C for the enzyme from V. harveyi. All the luciferases were significantly stabilized at increased salt concentrations, at low pH values, or in the presence of dithiothreitol (DTT) and EDTA. The addition of DTT and EDTA affected the reversible stage of enzyme inactivation, while salts reduced the rate of the irreversible stage. A peak corresponding to aggregated protein was detected by gel chromatography of irreversibly inactivated luciferase. Activation energies were calculated for each luciferase in bioluminescent reactions with decanal, dodecanal, tetradecanal, and without aldehydes. The activation energy of the reaction with tetradecanal was much lower than those with the other aldehydes. The temperature dependence of the lifetime of the long-lived reaction intermediate showed that in the 10-30 degrees C interval all the luciferases, except for the enzyme from V. harveyi, have only one active form.

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

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

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12.

Entropy approach in the analysis of anisotropy of digital images [Text] / E. N. Kirsanova, M. G. Sadovsky // Open Syst. Inf. Dyn. - 2002. - Vol. 9, Is. 3. - P. 239-250, DOI 10.1023/A:1019704411382. - Cited References: 15 . - ISSN 1230-1612

РУБ Thermodynamics + Computer Science, Information Systems + Mathematics, Applied + Mechanics + Physics, Mathematical + Statistics & Probability

Аннотация: Anisotropy is assumed to be the difference of a plane object observed in different dimensions. For digital images, anisotropy is determined in two ways. The first one is based on the comparison of mosaics bearing rectangular smalts developed in different (perpendicular, to be exact) directions. The comparison is provided through an intermediate mosaic called palette, that is the mosaic with the frequency of smalts equal to arithmetic mean of the frequency of smalts of compared mosaics. The latter is based on the calculation of the information capacity of the mosaics developed in different directions. The information capacity is the specific entropy of real mosaic calculated against the reconstructed one bearing the most probable expansions of smaller smalts. The problem of test object is discussed.

WOS
Держатели документа:
Krasnoyarsk State Tech Univ, Krasnoyarsk 660074, Russia
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kirsanova, E.N.; Sadovsky, M.G.

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13.

Effect of season and trophic level on fatty acid composition and content of four commercial fish species from Krasnoyarsk Reservoir (Siberia, Russia) / N. N. Sushchik, A. E. Rudchenko, M. I. Gladyshev // Fish. Res. - 2017. - Vol. 187. - P178-187, DOI 10.1016/j.fishres.2016.11.016 . - ISSN 0165-7836
Кл.слова (ненормированные):
Fatty acids -- Piscivorous and omnivorous fish -- Season -- Stable isotopes -- Trophic level
Аннотация: Two groups of factors, phylogenetic and ecological, are presently regarded as controlling fatty acid composition of fish, including essential eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids. Environmental effects, e.g., trophic position, temperature and/or seasonality, were previously studied using sums of fatty acids or only their level data. We tested the hypothesis that differences in trophic levels of piscivorous (pike and perch) and omnivorous (roach and bream) fish from a mesotrophic reservoir allow discriminating levels and contents of individual fatty acids, especially EPA and DHA. The more established measurements, i.e., stomach contents and carbon and nitrogen stable isotopes in fish muscles, were also carried out to provide linkages between the different ecological tracers, fatty acids versus stable isotopes, and matching the methods for long-term food sources (fatty acids and stable isotopes) and recent foraging (stomach content analysis). We also studied a putative influence of seasonality. Similar to other studies, there were seasonal changes in fatty acid composition and contents of two fish, perch and roach, due to direct and indirect effects of water temperature. Meanwhile, the piscivorous and omnivorous species captured in the same month, were explicitly differentiated on a base of stable isotopes and fatty acids. Significantly higher percentages and contents of DHA in piscivorous fish, perch and pike, relatively to those in roach and bream, likely indicated a higher trophic transfer efficiency for this essential fatty acid. All the fishes have commercial importance for regional fishery and are harvested from the studied reservoir for human nutrition. Regarding content of EPA + DHA (mg g?1 fish) as the indicator of nutritive value for humans, pike had the highest nutritive value, roach and perch had intermediate overlapped values, and bream was of the least benefit. © 2016 Elsevier B.V.

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Держатели документа:
Institute of Biophysics of Federal Research Center “Krasnoyarsk Science Center” of Siberian Branch of Russian Academy of Sciences, Akademgorodok, 50/50, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny av, 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Sushchik, N. N.; Rudchenko, A. E.; Gladyshev, M. I.

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14.

Mechanism and color modulation of fungal bioluminescence / Z. M. Kaskova [et al.] // Sci. Adv. - 2017. - Vol. 3, Is. 4. - Ст. e1602847, DOI 10.1126/sciadv.1602847. - Cited References:40. - This work was supported by the Sao Paulo Research Foundation [FAPESP grants 10/11578-5 (to A.G.O.), 13/16885-1 (to C.V.S.), 14/14866-2 (to E.L.B.), 13/07914-8 (to E.P. and F.A.D.), and 2012/12663-1 (to P.D.M.) and CEPID Redoxoma 2013/07937-8 (to P.D.M.)], the National Council for Scientific and Technological Development (CNPq) [301307/2013-0 (to P.D.M.)], NAP Redoxoma (PRPUSP) [2011.1.9352.1.8. (to P.D.M.)], the Japan Society for the Promotion of Science Grants-in-Aid for Scientific Research (KAKENHI) [grant no. 16K07715 (to Y.O.)], Chubu University [grant AII28II M01 (to Y.O.)], and the Russian Science Foundation (grant 16-14-00052 to all Russian authors). . - ISSN 2375-2548

РУБ Multidisciplinary Sciences
Рубрики:
SINGLET MOLECULAR-OXYGEN
QUANTUM YIELDS
CHEMILUMINESCENCE
Аннотация: Bioluminescent fungi are spread throughout the globe, but details on their mechanism of light emission are still scarce. Usually, the process involves three key components: an oxidizable luciferin substrate, a luciferase enzyme, and a light emitter, typically oxidized luciferin, and called oxyluciferin. We report the structure of fungal oxyluciferin, investigate the mechanism of fungal bioluminescence, and describe theuseof simple synthetic alpha-pyrones as luciferins to produce multicolor enzymatic chemiluminescence. A high-energy endoperoxide is proposed as an intermediate of the oxidation of the native luciferin to the oxyluciferin, which is a pyruvic acid adduct of caffeic acid. Luciferase promiscuity allows the use of simple alpha-pyrones as chemiluminescent substrates.

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Russian Acad Sci, Inst Bioorgan Chem, Miklukho Maklaya 16-10, Moscow 117997, Russia.
Pirogov Russian Natl Res Med Univ, OStrovitianov 1, Moscow 117997, Russia.
SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Univ Sao Paulo, Fac Ciencias Farmaceut, Dept Anal Clin & Toxicolgicas, BR-05508900 Sao Paulo, Brazil.
Nagoya Univ, Grad Sch Bioagr Sci, Nagoya, Aichi 4648601, Japan.
Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05508900 Sao Paulo, Brazil.
Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, BR-05508900 Sao Paulo, Brazil.
Univ Sao Paulo, Inst Oceanografico, Dept Oceanografia Fis Quim & Geol, BR-05508120 Sao Paulo, Brazil.
Chubu Univ, Dept Environm Biol, Kasugai, Aichi 4878501, Japan.

Доп.точки доступа:
Kaskova, Zinaida M.; Dorr, Felipe A.; Petushkov, Valentin N.; Purtov, Konstantin V.; Tsarkova, Aleksandra S.; Rodionova, Natalja S.; Mineev, Konstantin S.; Guglya, Elena B.; Kotlobay, Alexey; Baleeva, Nadezhda S.; Baranov, Mikhail S.; Arseniev, Alexander S.; Gitelson, Josef I.; Lukyanov, Sergey; Suzuki, Yoshiki; Kanie, Shusei; Pinto, Ernani; Di Mascio, Paolo; Waldenmaier, Hans E.; Pereira, Tatiana A.; Carvalho, Rodrigo P.; Oliveira, Anderson G.; Oba, Yuichi; Bastos, Erick L.; Stevani, Cassius V.; Yampolsky, Ilia V.; Sao Paulo Research Foundation [FAPESP] [10/11578-5, 13/16885-1, 14/14866-2, 13/07914-8, 2012/12663-1]; CEPID Redoxoma [2013/07937-8]; National Council for Scientific and Technological Development (CNPq) [301307/2013-0]; NAP Redoxoma (PRPUSP) [2011.1.9352.1.8]; Japan Society for the Promotion of Science [16K07715]; Chubu University [AII28II M01]; Russian Science Foundation [16-14-00052]

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15.

Fluorescence lifetime components reveal kinetic intermediate states upon equilibrium denaturation of carbonic anhydrase II / E. V. Nemtseva [et al.] // Methods Appl. Fluoresc. - 2018. - Vol. 6, Is. 1. - Ст. 015006, DOI 10.1088/2050-6120/aa994a. - Cited References:28. - The study of time-resolved protein fluorescence was supported by the Ministry for Science and Education of the Russian Federation (project 6.7734.2017/BCH). Kinetic and genetic engineering studies of carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. . - ISSN 2050-6120

РУБ Chemistry, Analytical + Chemistry, Physical
Рубрики:
PROTEIN FLUORESCENCE
   TRYPTOPHAN PROTEINS
   RESIDUES
   STABILITY
Кл.слова (ненормированные):
time-resolved fluorescence spectroscopy -- carbonic anhydrase II -- protein -- intermediate states -- comparison of kinetic and equilibrium experiments -- protein fluorescence lifetime
Аннотация: In most cases, intermediate states of multistage folding proteins are not 'visible' under equilibrium conditions but are revealed in kinetic experiments. Time-resolved fluorescence spectroscopy was used in equilibrium denaturation studies. The technique allows for detecting changes in the conformation and environment of tryptophan residues in different structural elements of carbonic anhydrase II which in its turn has made it possible to study the intermediate states of carbonic anhydrase II under equilibrium conditions. The results of equilibrium and kinetic experiments using wild-type bovine carbonic anhydrase II and its mutant form with the substitution of leucine for alanine at position 139 (L139A) were compared. The obtained lifetime components of intrinsic tryptophan fluorescence allowed for revealing that, the same as in kinetic experiments, under equilibrium conditions the unfolding of carbonic anhydrase II ensues through formation of intermediate states.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia.

Доп.точки доступа:
Nemtseva, Elena V.; Lashchuk, Olesya O.; Gerasimova, Marina A.; Melnik, Tatiana N.; Nagibina, Galina S.; Melnik, Bogdan S.; Ministry for Science and Education of the Russian Federation [6.7734.2017/BCH]; Russian Science Foundation [N14-24-00157]

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16.

Screening of biopolymeric materials for cardiovascular surgery toxicity—Evaluation of their surface relief with assessment of morphological aspects of monocyte/macrophage polarization in atherosclerosis patients / N. G. Menzyanova [et al.] // Toxicol. Rep. - 2019. - Vol. 6. - P74-90, DOI 10.1016/j.toxrep.2018.11.009 . - ISSN 2214-7500
Кл.слова (ненормированные):
Atherosclerosis -- Cell morphology -- Intravascular stenting -- Macrophages -- Monocytes -- Polyhydroxyalkanoates
Аннотация: The morphotypes of human macrophages (MPh) were studied in the culture on nano-structured biopolymer substrates, made from polyhydroxyalcanoates (PHAs) of five various monomer compositions, followed by the solvent evaporation. Its surface relief, which was further in direct contact with human cells in vitro, was analyzed by atomic force microscopy (AFM) and scanning electron microscopy (SEM). It was shown, that the features of the micro/nano relief depend on the monomeric composition of the polymer substrates. Monocytes (MN) of patients with atherosclerosis and cardiac ischemia, undergoing stenting and conventional anti-atherosclerotic therapy, were harvested prior and after stenting. MN were isolated and cultured, with the transformation into MPh in direct contact with biopolymer culture substrates with different monomer composition and nano-reliefs, and transformed into MPh, in comparison with the same process on standard culture plastic. Sub-populations of cells with characteristic morphology in each phenotypic class were described, and their quantitative ratios for each sample of polymers were counted as an intermediate result in the development of “smart” material for cardiovascular devices. The results obtained allow us to assume, that the processes of MPh differentiation and polarization in vitro depend not only on the features of the micro/nano relief of biopolymer substrates, but also on the initial state of MN in vivo and general response of patients. © 2018 The Authors

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Держатели документа:
Siberian Federal University, 79, Svobodny av., Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, 50/50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
L.V. Kirensky Institute of Physics, Siberian Branch of the Russian Academy of Sciences, 50/38 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Federal Research Center Krasnoyarsk Scientific Center of the Siberian Branch of the Russian Academy of Sciences, 50 Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Federal Center for Cardiovascular Surgery, 45 Karaulnaya, Krasnoyarsk, 660020, Russian Federation

Доп.точки доступа:
Menzyanova, N. G.; Pyatina, S. А.; Nikolaeva, E. D.; Shabanov, A. V.; Nemtsev, I. V.; Stolyarov, D. P.; Dryganov, D. B.; Sakhnov, E. V.; Shishatskaya, E. I.

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17.

Structural transitions of photobacterium leiognathi luciferase determined by various optical techniques under urea-induced equilibrium denaturation / D. V. Gulnov [и др.] // Tsitologiya. - 2018. - Vol. 60, Is. 10. - С. 847-850, DOI 10.7868/S0041377118100181 . - ISSN 0041-3771
Кл.слова (ненормированные):
Bacterial luciferase -- Circular dichroism -- Denaturation -- Protein fluorescence lifetime -- Protein intermediate states
Аннотация: The study was aimed to identification of conformational transitions of Photobacterium leiognathi luciferase during equilibrium denaturation with urea using several optical techniques, including circular dichroism, stationary and time-resolved fluorescence. Gravity center and intensity ratio I 325 /I 390 for the fluorescence spectra, molar ellipticity at 222 nm and fluorescence lifetimes of the protein were analyzed. Investigated parameters revealed two possible transitions for P. leiognathi luciferase with the midpoints at 0.5—1.1 and 3.5—4.2 M of urea. Changes in the values of two lifetime components, characterizing the luciferase fluorescence reflect both transitions, while steady-state fluorescence parameters (gravity center of spectrum and I 325 /I 390 ratio) reveal only the second one. Far-UV circular dichroism spectra displayed transitions at 4.2 M of urea for P. leiognathi luciferase. Conformational transitions characteristics of P. leiognathi luciferase and previously studied Vibrio harveyi luciferase (Inlow et al., 2002) were compared. Since, according to the published data for V. harveyi, midpoint of the second conformational transition is at about 2.5 M of urea, the results indicate more stable secondary structure for the P. leiognathi luciferase under study. The possible reasons for observed differences in fluorescent characteristics of two types of luciferases during denaturation can be connected to the microenvironment variation of the tryptophan residues in their tertiary structure, namely in position 131 and 277 in a-subunit. © 2018 Sankt Peterburg. All rights reserved.

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Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Gulnov, D. V.; Nemtseva, E. V.; Gerasimova, M. A.; Kratasyuk, V. A.

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18.

Radioactive particles in the Yenisei River floodplain (Russia): Characterization, leaching and potential effects in the environment / A. Bolsunovsky, M. Melgunov // J. Environ. Radioact. - 2019. - Vol. 208-209, DOI 10.1016/j.jenvrad.2019.105991 . - ISSN 0265-931X
Кл.слова (ненормированные):
Fuel particles -- Incidents at plutonium reactors -- Leaching experiments -- Low doses -- Plant bioassays -- The Yenisei river floodplain -- Aquatic ecosystems -- Aquatic organisms -- Banks (bodies of water) -- Floods -- Fuel gages -- Fuels -- Gamma rays -- Leaching -- Plutonium -- Radiation effects -- Radioactivity -- Radioisotopes -- Flood plains -- Fuel particles -- Leaching experiments -- Low dose -- Plant bioassays -- Rivers -- Elodea canadensis
Аннотация: The operation of the Mining-and-Chemical Combine (MCC), the largest producer of weapons-grade plutonium in Russia, has resulted in radioactive contamination of the Yenisei River floodplain. Investigations carried out in Novosibirsk and Krasnoyarsk institutes have shown that the floodplain of the Yenisei downstream of the MCC is contaminated by radioactive particles (RP) of various types and activities. Analytical characterization of the RP showed that most of them were fuel particles, which were carried into the Yenisei after incidents at the MCC reactors. The plutonium and caesium isotope ratios (238Pu/239,240Pu; 137Cs/134Cs) vary substantially between the particles, indicating different source terms and time intervals when the RP were formed. In addition to fuel RP, there were particles that contained activation radionuclides. The experiment on dissolution of RP using the model solution (the simulated stomach fluid) showed different cumulative extractions of radionuclides from the particles: 60Co and 137Cs extractions were the lowest, the extracted fractions of europium and americium isotopes were the largest, and plutonium occupied an intermediate position. High concentrations of radionuclides in RP are sources of exposure of organisms in aquatic and terrestrial ecosystems to low radiation doses. The plant bioassays of the effects of ?-radiation from RP showed the effect of low doses of ?-radiation on growth parameters of aquatic plant Elodea canadensis growing in the Yenisei River floodplain. The presence of RP from different sources in the Yenisei River floodplain makes this region a unique site for studying environmental effects of the particles. © 2019 Elsevier Ltd

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Institute of Biophysics Siberian Branch of Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Institute of Geology and Mineralogy Siberian Branch of Russian Academy of Sciences, Novosibirsk, 630090, Russian Federation

Доп.точки доступа:
Bolsunovsky, A.; Melgunov, M.

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19.

Viscous Media Slow Down the Decay of the Key Intermediate in Bacterial Bioluminescent Reaction / A. E. Lisitsa, L. A. Sukovatyi, V. A. Kratasyuk, E. V. Nemtseva // Doklad. Biochem. Biophys. - 2020. - Vol. 492, Is. 1. - P162-165, DOI 10.1134/S1607672920020106 . - ISSN 1607-6729
Кл.слова (ненормированные):
bacterial luciferase -- bioluminescence -- diffusional restriction -- enzyme reaction intermediate -- molecular dynamics method -- stopped-flow technique -- viscous microenvironment
Аннотация: Abstract: The effects of medium viscosity on the decay rate of the 4a-hydroperoxyflavin intermediate of the bioluminescent reaction was investigated. It was found that at low concentrations of glycerol or sucrose (viscosity 1.1–1.3 cP) the decay rate rises, whereas a further increase in viscosity to 6.2 cP leads to a decrease in the decay rate following a power function with an exponent of 0.82–0.84. Using molecular dynamics methods, it was shown that the presence of glycerol and sucrose molecules causes a change in the mobility of the amino acid residues in the active center of luciferase, particularly those responsible for binding of flavin. The results obtained are indicative of two opposite effects of viscous media with glycerol and sucrose: (1) destabilization of 4a-hydroperoxyflavin due to a change in the structural and dynamic properties of the protein and (2) stabilization of this intermediate by the decrease in the diffusion rate of its decay products. © 2020, Pleiades Publishing, Ltd.

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

Доп.точки доступа:
Lisitsa, A. E.; Sukovatyi, L. A.; Kratasyuk, V. A.; Nemtseva, E. V.

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20.

Viscous Media Slow Down the Decay of the Key Intermediate in Bacterial Bioluminescent Reaction / A. E. Lisitsa, L. A. Sukovatyi, V. A. Kratasyuk, E. V. Nemtseva // Dokl. Biochem. Biophys. - 2020. - Vol. 492, Is. 1. - P162-165, DOI 10.1134/S1607672920020106. - Cited References:15. - This work was supported by the Ministry of Science and Higher Education of the Russian Federation (project nos. 6.7734.2017 and 01201351504). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
LUCIFERASE
Кл.слова (ненормированные):
bacterial luciferase -- bioluminescence -- viscous microenvironment -- stopped-flow technique -- molecular dynamics method -- enzyme reaction -- intermediate -- diffusional restriction
Аннотация: The effects of medium viscosity on the decay rate of the 4a-hydroperoxyflavin intermediate of the bioluminescent reaction was investigated. It was found that at low concentrations of glycerol or sucrose (viscosity 1.1-1.3 cP) the decay rate rises, whereas a further increase in viscosity to 6.2 cP leads to a decrease in the decay rate following a power function with an exponent of 0.82-0.84. Using molecular dynamics methods, it was shown that the presence of glycerol and sucrose molecules causes a change in the mobility of the amino acid residues in the active center of luciferase, particularly those responsible for binding of flavin. The results obtained are indicative of two opposite effects of viscous media with glycerol and sucrose: (1) destabilization of 4a-hydroperoxyflavin due to a change in the structural and dynamic properties of the protein and (2) stabilization of this intermediate by the decrease in the diffusion rate of its decay products.

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

Доп.точки доступа:
Lisitsa, A. E.; Sukovatyi, L. A.; Kratasyuk, V. A.; Nemtseva, E. V.; Ministry of Science and Higher Education of the Russian Federation [6.7734.2017, 01201351504]

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