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Protein-protein complexation in bioluminescence [Text] / M. S. Titushin [et al.] // Protein Cell. - 2011. - Vol. 2, Is. 12. - P957-972, DOI 10.1007/s13238-011-1118-y. - Cited References: 114. - The work was funded by "Fellowship for Young International Scientists" of Chinese Academy of Sciences. This work was supported by the National Natural Science Foundation of China (Grant Nos: 30870483, 31070660, 31021062 and 81072449), Ministry of Science and Technology of China (Nos. 2009DFB30310, 2009CB918803 and 2011CB911103), CAS Research Grants (Nos. YZ200839 and KSCX2-EW-J-3). . - ISSN 1674-800X

РУБ Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
   LUCIFERIN-BINDING-PROTEIN
   RENILLA-RENIFORMIS LUCIFERASE
   VIBRIO-FISCHERI Y1
   JELLYFISH CLYTIA-GREGARIA
   ALPHA/BETA-HYDROLASE FOLD
   AMINO-ACID-SEQUENCE
   BACTERIAL LUCIFERASE
   ENERGY-TRANSFER
   CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
green-fluorescent protein (GFP) -- photoprotein -- luciferase -- lumazine protein -- Forster resonance energy transfer (FRET) -- docking
Аннотация: In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca2+-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of X-ray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

Держатели документа:
[Titushin, Maxim S.
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Feng, Yingang] Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Feng, Y.G.; Lee, J...; Vysotski, E.S.; Liu, Z.J.

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

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

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

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

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LC-MS and microscale NMR analysis of luciferin-related compounds from the bioluminescent earthworm Fridericia heliota / S. M. Marques [et al.] // Journal of Photochemistry and Photobiology B: Biology. - 2011. - Vol. 102, Is. 3. - P218-223, DOI 10.1016/j.jphotobiol.2010.12.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Fridericia heliota -- Luciferin -- Microscale NMR -- RP-HPLC-MS -- alkene -- alkyl group -- benzothiazole -- carboxylic acid -- hydroxyl group -- luciferin -- pterin -- absorption -- article -- bioluminescence -- earthworm -- Fridericia heliota -- isomer -- molecular weight -- nonhuman -- nuclear magnetic resonance -- priority journal -- reversed phase high performance liquid chromatography -- ultraviolet radiation -- Animals -- Chromatography, High Pressure Liquid -- Chromatography, Reverse-Phase -- Firefly Luciferin -- Luminescent Agents -- Magnetic Resonance Spectroscopy -- Mass Spectrometry -- Oligochaeta -- Fridericia heliota
Аннотация: This paper presents the main results of RP-HPLC-MS and microscale NMR analysis performed on Accompanying similar to Luciferin (AsLn(x)), compounds present in extracts of the bioluminescent earthworm Fridericia heliota that display similarities with Fridericia's luciferin, the substrate of the bioluminescent reaction. Three isomers of AsLn were discovered, AsLn(1), AsLn(2) and AsLn(3), all of which present a molecular weight of 529 Da. Their UV-Vis absorption spectra show maxima at 235 nm for AsLn(1), 238 and 295 nm for AsLn(2) and 241 and 295 nm for AsLn(3). MS n fragmentation patterns suggest the existence of carboxylic acid and hydroxyl moieties, and possibly chemical groups found in other luciferins like pterin or benzothiazole. The major isomer, AsLn(2), presents an aromatic ring and alkene and alkyl moieties. These luciferin-like compounds can be used as models that could give further insights into the structure of this newly discovered luciferin. В© 2010 Elsevier Inc. All rights reserved.

Scopus
Держатели документа:
Department of Chemistry and Biochemistry, Faculty of Sciences, Universidade Do Porto, Rua do Campo Alegre 687, 4169-007 Porto, Portugal
Laboratory of Photobiology, Institute of Biophysics, Russian Academy of Sciences, Akademgorodok, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Marques, S.M.; Petushkov, V.N.; Rodionova, N.S.; Esteves Da Silva, J.C.G.

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Purification and partial spectral characterization of a novel luciferin from the luminous enchytraeid Fridericia heliota / V. N. Petushkov, N. S. Rodionova // Journal of Photochemistry and Photobiology B: Biology. - 2007. - Vol. 87, Is. 2. - P130-136, DOI 10.1016/j.jphotobiol.2007.03.006 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Enchytraeid -- Luciferase -- Luciferin -- adenosine triphosphate -- luciferase -- luciferin -- animal cell -- anion exchange chromatography -- annelid worm -- article -- controlled study -- earthworm -- firefly -- luminance -- luminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- radiation absorption -- reversed phase liquid chromatography -- ultraviolet radiation -- Adenosine Triphosphate -- Animals -- Luciferases -- Luminescent Agents -- Oligochaeta -- Spectrum Analysis -- Enchytraeidae -- Fridericia heliota
Аннотация: A homogeneous luciferin preparation has been obtained from the luminous soil enchytraeid Fridericia heliota, which has an ATP-dependent luminescent system. A procedure for luciferin purification without losing fractions of active luciferase has been developed. The luciferin specific activity is 4000 times increased; its UV absorption spectrum maximum is 294 nm with a local minimum at 262 nm. The luciferin of the enchytraeid F. heliota is significantly different from firefly luciferin, whose luminescent reaction also requires ATP, and it also appears to have no similarities to other known luciferins. В© 2007 Elsevier B.V. All rights reserved.

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

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

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

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

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

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ATP is a cosubstrate of the luciferase of the earthworm Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar', V. N. Petushkov // Doklady Biochemistry and Biophysics. - 2003. - Vol. 392, Is. 1-6. - P253-255, DOI 10.1023/A:1026134628735 . - ISSN 1607-6729
Кл.слова (ненормированные):
adenosine diphosphate -- adenosine phosphate -- adenosine triphosphate -- luciferase -- luciferin -- magnesium -- animal cell -- article -- controlled study -- earthworm -- hydrolysis -- luminescence -- nonhuman -- Adenosine Diphosphate -- Adenosine Triphosphate -- Animals -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Magnesium -- Oligochaeta -- Substrate Specificity -- Animalia -- Annelida -- Clitellata -- Enchytraeidae -- Pheretima sieboldi

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

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

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

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

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

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CompX, a luciferin-related tyrosine derivative from the bioluminescent earthworm Fridericia heliota. Structure elucidation and total synthesis / V. N. Petushkov [et al.] // Tetrahedron Letters. - 2014. - Vol. 55, Is. 2. - P460-462, DOI 10.1016/j.tetlet.2013.11.064 . - ISSN 0040-4039
Кл.слова (ненормированные):
Bioluminescence -- Enchytraeid -- Luciferin -- Total synthesis
Аннотация: A luciferin analog, CompX, was isolated from the extracts of the bioluminescent earthworm Fridericia heliota. Its structure was determined as (Z)-5-(2-carboxy-2-methoxyvinyl)-2-hydroxybenzoic acid by spectroscopic data analysis and was confirmed by total synthesis. The (Z)-configuration of the double bond was established by comparing the ROESY spectra of CompX with those of its synthetic (E)-isomer. CompX represents a tyrosine analog, not previously found in natural sources, and is probably derived from tyrosine by deamination, O-methylation of the resulting alpha-keto acid, and carboxylation at the aromatic core. © 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.; Tsarkova, A.S.; Dubinnyi, M.A.; Rodionova, N.S.; Marques, S.M.; Esteves Da Silva, J.C.G.; Shimomura, O.; Yampolsky, I.V.

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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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10.

A novel ATP-dependent bioluminescent system from the Siberian earthworm Fridericia heliota: structure elucidation of luciferin and its analogs [Text] / V. . Petushkov [et al.] // Luminescence. - 2014. - Vol. 29. - P54-55. - Cited References: 3 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Dubinnyi, Maxim
Tsarkova, Aleksandra
Baranov, Mikhail
Yampolsky, Ilia] Russian Acad Sci, Inst Bioorgan Chem, Moscow, Russia
[Petushkov, Valentin
Rodionova, Natalja
Shimomura, Osamu] Russian Acad Sci, Inst Biophys, Lab Photobiol, Siberian Branch, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V...; Dubinnyi, M...; Tsarkova, A...; Rodionova, N...; Baranov, M...; Shimomura, O...; Yampolsky, I...

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11.

A Novel Type of Luciferin from the Siberian Luminous Earthworm Fridericia heliota: Structure Elucidation by Spectral Studies and Total Synthesis [Text] / V. N. Petushkov [et al.] // Angew. Chem.-Int. Edit. - 2014. - Vol. 53, Is. 22. - P5566-5568, DOI 10.1002/anie.201400529. - Cited References: 13. - We thank Dr. Alexander O. Chizhov for recording mass spectra and Dr. K. S. Mineev for NMR analysis of synthetic intermediates. We acknowledge support from the Program of the Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11. G34.31.0058), the programs MCB RAS, President of the Russian Federation "Leading science school" (grant 3951.2012.4) and the Russian Foundation for Basic Research (grant 14-03-01015). B. M. S. was supported by a stipend from the Program of the President of the Russian Federation. . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
BIOLUMINESCENT EARTHWORM
Кл.слова (ненормированные):
bioluminescence -- luciferin -- natural products -- NMR spectroscopy -- total synthesis
Аннотация: The structure elucidation and synthesis of the luciferin from the recently discovered luminous earthworm Fridericia heliota is reported. This luciferin is a key component of a novel ATP-dependent bioluminescence system. UV, fluorescence, NMR, and HRMS spectroscopy studies were performed on 0.005 mg of the isolated substance and revealed four isomeric structures that conform to spectral data. These isomers were chemically synthesized and one of them was found to produce light when reacted with a protein extract from F. heliota. The novel luciferin was found to have an unusual extensively modified peptidic nature, thus implying an unprecedented mechanism of action.

WOS
Держатели документа:
[Petushkov, Valentin N.
Rodionova, Natalja S.
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Petushkov, Valentin N.
Rodionova, Natalja S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
[Dubinnyi, Maxim A.
Tsarkova, Aleksandra S.
Baranov, Mikhail S.
Kublitski, Vadim S.
Yampolsky, Ilia V.] Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Dubinnyi, M.A.; Tsarkova, A.S.; Rodionova, N.S.; Baranov, M.S.; Kublitski, V.S.; Shimomura, O...; Yampolsky, I.V.; Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" [11. G34.31.0058]; programs MCB RAS; Russian Federation "Leading science school" [3951.2012.4]; Russian Foundation for Basic Research [14-03-01015]; Russian Federation

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12.

On the quenching of bacterial luminescence by dyes [Текст] / Y. P. Meshalkin [и др.] // Biofizika. - 1999. - Vol. 44, Is. 6. - P. 1083-1087. - Cited References: 5 . - ISSN 0006-3029

РУБ Biophysics

Кл.слова (ненормированные):
bacterial luminescence -- dyes -- quenching
Аннотация: It was shown that the addition of dyes (sodium fluorescein, rhodamine 6G, unsubstituted rhodamine) to a bienzymic reaction mixture. (luciferin-luciferase. complex): leads to a decrease: in fluorescence intensity and the appearance of the dye fluorescence band. A similar effect was observed when the luciferin-luciferase complex and dye molecules were separated by distances considerably. exceeding the Forster radius of transfer. It is assumed that the mechanism of dye. fluorescence is not related to the excitation energy resonance transfer but is based on the excitation of dye molecules due to direct absorption of quanta of bacterial bioluminescence.

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

Доп.точки доступа:
Meshalkin, Y.P.; Nemtseva, E.V.; Alfimov, E.E.; Kudryasheva, N.S.

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13.

Model of the active site of firefly luciferase [Text] / T. P. Sandalova, N. N. Ugarova // Biochem.-Moscow. - 1999. - Vol. 64, Is. 8. - P. 962-967. - Cited References: 20 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
ESCHERICHIA-COLI
   SEQUENCE
   CLONING
   ENZYME
   CDNA
   SUPERFAMILY
Кл.слова (ненормированные):
bioluminescence -- firefly luciferase -- ATP -- luciferin -- spatial structure -- active site -- enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Karolinska Inst, S-17177 Stockholm, Sweden
Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sandalova, T.P.; Ugarova, N.N.

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14.

Novel Peptide Chemistry in Terrestrial Animals: Natural Luciferin Analogues from the Bioluminescent Earthworm Fridericia heliota [Text] / M. A. Dubinnyi [et al.] // Chem.-Eur. J. - 2015. - Vol. 21, Is. 10. - P3942-3947, DOI 10.1002/chem.201406498. - Cited References:17. - We thank Dr. K. V. Antonov for registration of LC-HRMS spectra. This work was supported by the Russian Science Foundation grant 14-50-00131. . - ISSN 0947-6539. - ISSN 1521-3765

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
DERIVATIVES
IDENTIFICATION
Кл.слова (ненормированные):
bioluminescence -- Fridericia heliota -- luciferin -- peptides -- structure -- elucidation
Аннотация: We report isolation and structure elucidation of AsLn5, AsLn7, AsLn11 and AsLn12: novel luciferin analogs from the bioluminescent earthworm Fridericia heliota. They were found to be highly unusual modified peptides, comprising either of the two tyrosine-derived chromophores, CompX or CompY and a set of amino acids, including threonine, gamma-aminobutyric acid, homoarginine, and unsymmetrical N,N-dimethylarginine. These natural compounds represent a unique peptide chemistry found in terrestrial animals and rise novel questions concerning their biosynthetic origin.

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Scopus
Держатели документа:
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation
Laboratory of Photobiology, Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Dubinnyi, Maxim A.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Kovalchuk, Sergey I.; Ziganshin, Rustam H.; Baranov, Mikhail S.; Mineev, Konstantin S.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]

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15.

Total synthesis of AsLn2 - A luciferin analogue from the Siberian bioluminescent earthworm Fridericia heliota / A. S. Tsarkova [et al.] // Mendeleev Commun. - 2015. - Vol. 25, Is. 2. - P99-100, DOI 10.1016/j.mencom.2015.03.005 . - ISSN 0959-9436
Аннотация: Total synthesis of AsLn2, a luciferin analogue isolated from the Siberian bioluminescent earthworm F. heliota, was performed from (Z)-5-(2,3-dimethoxy-3-oxoprop-1-en-1-yl)-2-hydroxybenzoic acid in six steps. © 2015 Mendeleev Communications. Published by ELSEVIER B.V.

Scopus,
WOS
Держатели документа:
M. M. Shemyakin-Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of SciencesMoscow, Russian Federation
N. I. Pirogov Russian National Research Medical UniversityMoscow, Russian Federation
Institute of Fundamental Biology and Biotechnology, Siberian Federal UniversityKrasnoyarsk, Russian Federation
Institute of Biophysics, Siberian Branch of the Russian Academy of SciencesKrasnoyarsk, Russian Federation
'Drugs Technology' Ltd.Khimki, Moscow Region, Russian Federation
ИБФ СО РАН

Доп.точки доступа:
Tsarkova, A.S.; Dubinnyi, M.A.; Baranov, M.S.; Petushkov, V.N.; Rodionova, N.S.; Zagudaylova, M.B.; Yampolsky, I.V.

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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.

The Chemical Basis of Fungal Bioluminescence / K. V. Purtov [et al.] // Angew. Chem. Int. Ed. - 2015. - Vol. 54, Is. 28. - P8124-8128, DOI 10.1002/anie.201501779 . - ISSN 1433-7851
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- biosynthesis -- luciferin -- natural products -- Biochemistry -- Bioluminescence -- Biosynthesis -- Metabolites -- Phosphorescence -- Biochemical mechanisms -- Bioorganic chemistry -- luciferin -- Natural products -- Plant secondary metabolites -- Structural similarity -- Fungi
Аннотация: Many species of fungi naturally produce light, a phenomenon known as bioluminescence, however, the fungal substrates used in the chemical reactions that produce light have not been reported. We identified the fungal compound luciferin 3-hydroxyhispidin, which is biosynthesized by oxidation of the precursor hispidin, a known fungal and plant secondary metabolite. The fungal luciferin does not share structural similarity with the other eight known luciferins. Furthermore, it was shown that 3-hydroxyhispidin leads to bioluminescence in extracts from four diverse genera of luminous fungi, thus suggesting a common biochemical mechanism for fungal bioluminescence. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Scopus,
WOS
Держатели документа:
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation

Доп.точки доступа:
Purtov, K.V.; Petushkov, V.N.; Baranov, M.S.; Mineev, K.S.; Rodionova, N.S.; Kaskova, Z.M.; Tsarkova, A.S.; Petunin, A.I.; Bondar, V.S.; Rodicheva, E.K.; Medvedeva, S.E.; Oba, Y.; Arseniev, A.S.; Lukyanov, S.; Gitelson, J.I.; Yampolsky, I.V.

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18.

Coelenterazine-dependent luciferases / S. V. Markova, E. S. Vysotski // Biochemistry Moscow. - 2015. - Vol. 80, Is. 6. - P714-732, DOI 10.1134/S0006297915060073 . - ISSN 0006-2979
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- luciferin -- Coelenterata -- Cypridina luciferin -- Fungi -- Hexapoda -- Mollusca -- Protozoa
Аннотация: Bioluminescence is a widespread natural phenomenon. Luminous organisms are found among bacteria, fungi, protozoa, coelenterates, worms, molluscs, insects, and fish. Studies on bioluminescent systems of various organisms have revealed an interesting feature - the mechanisms underlying visible light emission are considerably different in representatives of different taxa despite the same final result of this biochemical process. Among the several substrates of bioluminescent reactions identified in marine luminous organisms, the most commonly used are imidazopyrazinone derivatives such as coelenterazine and Cypridina luciferin. Although the substrate used is the same, bioluminescent proteins that catalyze light emitting reactions in taxonomically remote luminous organisms do not show similarity either in amino acid sequences or in spatial structures. In this review, we consider luciferases of various luminous organisms that use coelenterazine or Cypridina luciferin as a substrate, as well as modifications of these proteins that improve their physicochemical and bioluminescent properties and therefore their applicability in bioluminescence imaging in vivo. © 2015 Pleiades Publishing, Ltd.

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

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

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19.

Creation of Artificial Luciferases to Expand their Analytical Potential [Text] / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929, DOI 10.2174/1386207318666150917100011. - Cited References:79. - The work was supported by: the RFBR grant No. 14-08-00902/14; the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1). . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
BIOLUMINESCENT REPORTER APPLICATIONS
COELENTERAZINE-BINDING PROTEIN
Кл.слова (ненормированные):
Luciferase -- luciferin -- photoprotein -- bioluminescence -- mutagenesis -- luciferase-based assay -- bioimaging -- reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescence-based analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Frank, Ludmila A.; RFBR [14-08-00902/14]; [VI 57.1.1]

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20.

Creation of artificial luciferases to expand their analytical potential / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioimaging -- Bioluminescence -- Luciferase -- Luciferase-based assay -- Luciferin -- Mutagenesis -- Photoprotein -- Reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescencebased analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnii ave., 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Frank, L. A.

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