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Application of Enzyme Bioluminescence for Medical Diagnostics [Text] / L. A. Frank, V. V. Krasitskaya // Adv. Biochem. Eng. Biotechnol. : SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - P175-197. - (Advances in Biochemical Engineering-Biotechnology), DOI 10.1007/978-3-662-43385-0_6. - Cited References:63 . -

РУБ Biotechnology & Applied Microbiology
Рубрики:
RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Кл.слова (ненормированные):
Bioluminescence -- Ca2+-regulated photoprotein -- Diagnostics -- Immunoassay -- Luciferase -- Nucleic acid hybridization assay
Аннотация: Nowadays luciferases are effectively used as analytical instruments in a great variety of research fields. Of special interest are the studies dealing with elaboration of novel analytical systems for the purposes of medical diagnostics. The ever-expanding spectrum of clinically important analytes accounts for the increasing demand for new techniques for their detection. In this chapter we have made an attempt to summarize the results on applications of luciferases as reporters in binding assays including immunoassay, nucleic acid hybridization assay, and so on. The data over the last 15 years have been analyzed and clearly show that luciferase-based assays, due to extremely high sensitivity, low cost, and the lack of need for skilled personnel, hold much promise for clinical diagnostics.

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

Доп.точки доступа:
Frank, Ludmila A.; Krasitskaya, Vasilisa V.

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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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Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy / E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 19. - Ст. 10449, DOI 10.3390/ijms221910449. - Cited References:45. - The research was partially funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by the RFBR and Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (projects No. 20-44-243002 and 20-44-240006); and by the RFBR (project No. 20-34-90118). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
TRYPTOPHAN FLUORESCENCE
   CRYSTAL-STRUCTURE
   SUBUNIT
   BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- urea-induced denaturation -- time-resolved -- spectroscopy -- conformational stability -- FRET -- tryptophan fluorescence -- molecular dynamics -- unfolding pathway
Аннотация: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of alpha-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Russia.

Доп.точки доступа:
Nemtseva, Elena, V; Gulnov, Dmitry, V; Gerasimova, Marina A.; Sukovatyi, Lev A.; Burakova, Ludmila P.; Karuzina, Natalya E.; Melnik, Bogdan S.; Kratasyuk, Valentina A.; Burakova, Lyudmila; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]; Krasnoyarsk Regional Fund of Science [20-44-243002, 20-44-240006]; RFBRRussian Foundation for Basic Research (RFBR)

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Bacterial luciferases from vibrio harveyi and photobacterium leiognathi demonstrate different conformational stability as detected by time-resolved fluorescence spectroscopy / E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 19. - Ст. 10449, DOI 10.3390/ijms221910449 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Conforma-tional stability -- FRET -- Molecular dynamics -- Time-resolved spectroscopy -- Tryptophan fluorescence -- Unfolding pathway -- Urea-induced denaturation
Аннотация: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of ?-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Photobiology Laboratory, Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142290, Russian Federation

Доп.точки доступа:
Nemtseva, E. V.; Gulnov, D. V.; Gerasimova, M. A.; Sukovatyi, L. A.; Burakova, L. P.; Karuzina, N. E.; Melnik, B. S.; Kratasyuk, V. A.

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Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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

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

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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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Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465, DOI 10.3390/ijms21207465. - Cited References:251. - The work was supported by the Russian State funded budget project of IBP SB RAS No. AAAA-A19-119031890015-0. . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
PROTEIN-PROTEIN INTERACTIONS
CA2+-REGULATED PHOTOPROTEIN OBELIN
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- Ca2+-regulated -- photoprotein -- analytical systems
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate-coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases.

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Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A.; Russian State funded budget project of IBP SB RAS [AAAA-A19-119031890015-0]

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Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications / V. V. Krasitskaya, E. E. Bashmakova, L. A. Frank // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 20. - Ст. 7465. - P1-31, DOI 10.3390/ijms21207465 . - ISSN 1661-6596
Кл.слова (ненормированные):
Analytical systems -- Bioluminescence -- Ca2+-regulated photoprotein -- Coelenterazine -- Luciferase
Аннотация: The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization—Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme–substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogues with new unique properties has led to the development of new experimental analytical methods based on them. The commercial availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of analytical methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biological research areas, which confirms them to be a powerful analytical tool. In this review, we consider the main directions, results, and achievements in research involving these luciferases. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation
School of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Bashmakova, E. E.; Frank, L. A.

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10.

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.

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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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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.

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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13.

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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14.

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.

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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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15.

High-active truncated luciferases of copepod Metridia longa and their characterization as secreted reporters inmammalian cells / S. V. Markova, L. P. Burakova, E. S. Vysotski // Luminescence. - 2012. - Vol. 27, Is. 2. - P138-139. - Cited References: 1 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
[Markova, Svetlana V.
Burakova, Ludmila P.
Vysotski, Eugene S.] Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Vysotski, Eugene S.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Vysotski, E.S.

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16.

INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE [Text] / T. P. SANDALOVA, N. A. TYULKOVA // Biochem.-Moscow. - 1992. - Vol. 57, Is. 6. - P. 552-558. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   REACTIVE SULFHYDRYL
   PHOTOBACTERIUM-LEIOGNATHI
   VIBRIO-HARVEYI
   BIOLUMINESCENCE
   SUBUNIT
   REGION
   GENE
Кл.слова (ненормированные):
LUCIFERASE -- N-ETHYLMALEIMIDE
Аннотация: The kinetics of inactivation of luciferases from four species of luminescent bacteria by the thiol reagent N-ethylmaleimide were investigated The dependencies of inactivation on ionic strength differed among the enzymes. Increasing the molarity of the buffer increased the rate of inactivation of all luciferases except that of Vibrio harveyi. Modification of Photobacterium phosphoreum luciferase decreased the maximal intensity of bioluminescence, whereas modification of Photobacterium leiognathi and Vibrio fischeri luciferases in high ionic strength buffers decreased the maximal intensity of bioluminescence and changed the luminescence decay rate constant. High ionic strength apparently alters the conformational states of the luciferases.

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

Доп.точки доступа:
SANDALOVA, T.P.; TYULKOVA, N.A.

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17.

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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18.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- anisotropy -- antenna -- article -- bioluminescence -- complex formation -- energy transfer -- enzyme active site -- enzyme kinetics -- nonhuman -- priority journal -- protein protein interaction -- spectroscopy -- vibrionaceae -- Bacterial Proteins -- Carrier Proteins -- Cloning, Molecular -- Dithionite -- Flavin Mononucleotide -- Kinetics -- Luciferases -- Luminescent Measurements -- Luminescent Proteins -- Models, Structural -- Photobacterium -- Protein Binding -- Protein Conformation -- Recombinant Proteins -- Spectrophotometry -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Photobacterium leiognathi -- Vibrio fischeri -- Vibrionaceae
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 can 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, where 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 for the protein- protein interaction in the absence of the aliphatic component.

Scopus
Держатели документа:
Department of Biochemistry, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Acad. of Sci. of Russia, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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19.

Kinetic analysis of bacterial water-organic media [Text] / I. E. Sukovataya, N. A. Tyulkova // Luminescence. - 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P. 271-273, DOI 10.1002/bio.649.abs. - Cited References: 10 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bacterial luciferase -- organic solvents -- Michaelis constant
Аннотация: The interaction of luciferases from two types of luminous bacteria, Photobacterium leiognathi and Vibrio harveyi, with their substrates [the photorecovered. FMNH2 and long-chain aldehydes-decanal (C-10), dodecanal (C-12) and tetradecanal (C-14)] in water-organic media was analysed using kinetic graphical methods. Moderate concentrations of organic solvents have been demonstrated to activate the bioluminescence, while higher concentrations inhibit it. The interactions of these effectors with luciferases show different types of kinetics, which depend on concentrations of solvents, kinds of enzymes and substrates. The apparent value of the Michaelis constant, K-m for C-14 of both luciferases and for C-10 of luciferase V. harveyi is enhanced with increasing concentration of the organic solvent, but K-m for C-12 and C-10 of luciferase P. leiognathi decreases. Obviously, at the specific binding of aldehydes with luciferases in the first case, hydrophobic interactions are realized, but in second, the electrostatic interactions are realized. The series of changes in parameters of bioluminescence reaction catalysed by different luciferases is obviously determined by their structural peculiarities. Copyright (C) 2001 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Sukovataya, I.E.; Tyulkova, N.A.

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20.

New types of luminescent systems of soil enchytraeids (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / V. N. Petushkov, N. S. Rodionova // Doklady Biochemistry and Biophysics. - 2005. - Vol. 401, Is. 1-6. - P115-118, DOI 10.1007/s10628-005-0047-1 . - ISSN 1607-6729
Кл.слова (ненормированные):
annelid worm -- article -- energy transfer -- epidermis cell -- luminescence -- nonhuman -- soil analysis -- Animals -- Luciferases -- Luminescence -- Oligochaeta -- Annelida -- Clitellata -- Enchytraeidae

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

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

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