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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): coelenterazine--2-hydroperoxy-coelenterazine--obelia longissima--renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : van Oort B..., Eremeeva E.V., Koehorst RBM, Laptenok S.P., van Amerongen H..., van Berkel WJH, Malikova N.P., Markova S.V., Vysotski E.S., Visser AJWG, Lee J...
Заглавие : Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin
Колич.характеристики :6 с
Коллективы : NATO Collaborative Linkage [979229]; RFBR [09-04-12-022]; 'Stichung voor Fundamenteel Onderzock der Materic (FOM)'; NWO; Wageningen University; European Community Marie Curie Research Training Network [MRTN-CT-2005-019481]; netherlands Organization [635 000 014]
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2009. - Vol. 48, Is. 44. - С. 10486-10491. - ISSN 0006-2960, DOI 10.1021/bi901436m
Примечания : Cited References: 33. - This work was supported by NATO Collaborative Linkage Grant No 979229,Grants of SB RAS and RFBR 09-04-12-022, MCB program of RAS BvO was supported by 'Stichung voor Fundamenteel Onderzock der Materic (FOM)', which is financially supported by the NWO. and by I Rubicon grant of NWO E V E was supported by Wageningen University Sandwich Ph D-Fellowship program S P L was supported by Wageningen University Sandwich Ph D.-Fellowship program, European Community Marie Curie Research Training Network MRTN-CT-2005-019481 (From FLIM to FLIN), and Computational Science Gram 635 000 014 from the netherlands Organization for Scientific Research
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
W92F OBELIN
COELENTERAZINE
MECHANISM
EXPRESSION
PROTEINS
Аннотация: Addition of calcium tons to the Ca(2+)-regulated photoproteins, such its aequorin and obelin, produces it blue bioluminescence originating from fluorescence transition of the protein-bound product coelenteramide. The kinetics of several transient fluorescent species of the bound coelenteramide is resolved after picosecond-laser excitation and streak camera detection. The Initially formed spectral distributions at picosecond-times are broad, evidently comprised of two contributions, One at higher energy (similar to 25 000 cm(-1)) assigned as from the Ca(2+)-discharged photoprotein-bound coelenteramide in its neutral state. This component decays much more rapidly (t(1/2) similar to 2 ps) in the case of the Ca(2+)-discharged obelin than aequorin (t(1/2) similar to 30 ps). The Second component at lower energy shows several intermediates in the 150-500 ps miles. with it Final species having spectral maxima 19 400 cm(-1), bound to Ca(2+)-discharged obelin. and 2 1300 cm(-1), bound to Ca(2+)-discharged aequorin, and both have it fluorescence decay lifetime of 4 ns It is proposed that the rapid kinetics of these fluorescence transients oil the picosecond time scale, correspond to times For relaxation of the protein Structural environment of the binding cavity
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M..., Gibson B.G., Lee J...
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive
Колич.характеристики :8 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 0006-2960, DOI 10.1021/bi9608931
Примечания : Cited References: 41
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eke G..., Kuzmina A.M., Goreva A.V., Shishatskaya E.I., Hasirci N..., Hasirci V...
Заглавие : In vitro and transdermal penetration of PHBV micro/nanoparticles
Колич.характеристики :11 с
Коллективы : Government of the Russian Federation [220, 11.G34.31.0013, MD-3112.2012.4]; EC FP7 SKINTREAT project; State Planning Organization (Turkey)
Место публикации : J. Mater. Sci.-Mater. Med.: SPRINGER, 2014. - Vol. 25, Is. 6. - С. 1471-1481. - ISSN 0957-4530, DOI 10.1007/s10856-014-5169-5. - ISSN 1573-4838
Примечания : Cited References: 38. - The study was supported by the Government of the Russian Federation (Decree No. 220 of 09.04.2010) (Agreement No. 11.G34.31.0013) and (Grant No MD-3112.2012.4). We gratefully acknowledge the EC FP7 SKINTREAT project and the State Planning Organization (Turkey) for the grant to establish BIOMATEN. Mr. A. Buyuksungur is acknowledged for his contributions with CLSM.
Предметные рубрики: DRUG-DELIVERY
PLGA NANOPARTICLES
CELLULAR UPTAKE
MICROPARTICLES
POLYHYDROXYALKANOATES
CYTOTOXICITY
SIZE
POLYESTERS
MECHANISM
CELLS
Аннотация: The purpose of this study was to develop micro and nano sized drug carriers from poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV), and study the cell and skin penetration of these particles. PHBV micro/nanospheres were prepared by o/w emulsion method and were stained with a fluorescent dye, Nile Red. The particles were fractionated by centrifugation to produce different sized populations. Topography was studied by SEM and average particle size and its distribution were determined with particle sizer. Cell viability assay (MTT) was carried out using L929 fibroblastic cell line, and particle penetration into the cells were studied. Transdermal permeation of PHBV micro/nanospheres and tissue reaction were studied using a BALB/c mouse model. Skin response was evaluated histologically and amount of PHBV in skin was determined by gas chromatography-mass spectrometry. The average diameters of the PHBV micro/nanosphere batches were found to be 1.9 mu m, 426 and 166 nm. Polydispersity indices showed that the size distribution of micro sized particles was broader than the smaller ones. In vitro studies showed that the cells had a normal growth trend. MTT showed no signs of particle toxicity. The 426 and 166 nm sized PHBV spheres were seen to penetrate the cell membrane. The histological sections revealed no adverse effects. In view of this data nano and micro sized PHBV particles appeared to have potential to serve as topical and transdermal drug delivery carriers for use on aged or damaged skin or in cases of skin diseases such as psoriasis, and may even be used in gene transfer to cells.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryasheva N.S., Nemtseva E.V., Sizykh A.G., Kratasyuk V.A., Visser AJWG
Заглавие : Estimation of energy of the upper electron-excited states of the bacterial bioluminescent emitter
Колич.характеристики :5 с
Место публикации : J. Photochem. Photobiol. B-Biol.: ELSEVIER SCIENCE SA, 2002. - Vol. 68, Is. 02.03.2013. - P88-92. - ISSN 1011-1344, DOI 10.1016/S1011-1344(02)00360-3
Примечания : Cited References: 25
Предметные рубрики: MECHANISM
Ключевые слова (''Своб.индексиров.''): bioluminescence--electron-excited states--energy transfer
Аннотация: The hypothesis of activity of the upper electron-excited states of the bacterial bioluminescent emitter was verified using dye molecules as foreign energy acceptors. Six compounds were selected having fluorescent state energies ranging from 25 700 to 32 000 cm(-1) (anthracene, pyrene, 1.4-bis(5-phenyloxasol-2-yl)benzene (POPOP), p-bis(o-methylstyryl)benzene (MSB), 2-methoxy-naphtalene, p-terphenyl), exceeding that of the bioluminescent emitter (22 000 cm(-1)). Their absorption spectra do not overlap with the bioluminescence spectrum; the trivial light absorption and the intermolecular resonance S-S energy transfer were excluded. Bacterial bioluminescent spectra of the coupled enzyme system NADH:FMN-oxidoreductase-luciferase in the presence of MSB were presented as an example. The weak sensitized fluorescence of MSB was registered. The results obtained have confirmed the activity of the energetic precursor in the bacterial bioluminescence. Its energy can be located in the interval of 26 000-27 000 cm(-1). (C) 2002 Published by Elsevier Science B.V.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kudryasheva N.S., Nemtseva E.V., Visser AJWG, van Hoek A...
Заглавие : Interaction of aromatic compounds with Photobacterium leiognathi luciferase: fluorescence anisotropy study
Колич.характеристики :6 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2003. - Vol. 18, Is. 3. - P156-161. - ISSN 1522-7235, DOI 10.1002/bio.719
Примечания : Cited References: 25
Предметные рубрики: ELECTRON-EXCITED-STATES
BACTERIAL BIOLUMINESCENCE
LUMAZINE PROTEIN
MECHANISM
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--fluorescent compounds--anisotropy decay
Аннотация: The time-resolved and steady-state fluorescence techniques,were employed to elucidate possible interactions of four aromatic compounds (anthracene, POPOP, MSB and 1,4-naphthalendiol) with bacterial luciferase. Fluorescence spectra and fluorescence anisotropy decays of these compounds were studied in ethanol, water-ethanol solutions and in the presence of bacterial luciferase. Shifts of fluorescent spectra and differences in rotational correlation times are interpreted in terms of weak (hydrophobic) interactions of the molecules with the enzyme. These interactions suggest the feasibility of intermolecular energy transfer by an exchange resonance mechanism with a collision-interaction radius as a way of excitation of these compounds in the reaction catalysed by bacterial luciferase. Copyright (C) 2003 John Wiley Sons, Ltd.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Dementyev D.V., Zotina T.A., Manukovsky N.S., Kalacheva G.S., Bolsunovsky, A. Ya.
Заглавие : Biosorption of Am-241 from aqueous solutions and its biochemical fractionation in Pleurotus ostreatus mycelium
Колич.характеристики :3 с
Коллективы : Russian Foundation for Basic Research [12-04-00915]
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2015. - Vol. 460, Is. 1. - С. 34-36. - ISSN 1607-6729, DOI 10.1134/S160767291501010X. - ISSN 1608-3091(eISSN)
Примечания : Cited References:11. - This work was supported by the Russian Foundation for Basic Research (project no. 12-04-00915).
Предметные рубрики: SACCHAROMYCES-CEREVISIAE
REMOVAL
AMERICIUM
MECHANISM
BIOMASS
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Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kotlobay, Alexey A., Dubinnyi, Maxim A., Purtov, Konstantin V., Guglya, Elena B., Rodionova, Natalja S., Petushkov, Valentin N., Bolt, Yaroslav V., Kublitski, Vadim S., Kaskova, Zinaida M., Ziganshin, Rustam H., Nelyubina, Yulia V., Dorovatovskii, Pavel V., Eliseev, Igor E., Branchini, Bruce R., Bourenkov, Gleb, Ivanov, Igor A., Oba, Yuichi, Yampolsky, Ilia V., Tsarkova, Aleksandra S.
Заглавие : Bioluminescence chemistry of fireworm Odontosyllis
Колич.характеристики :6 с
Коллективы : Russian Science FoundationRussian Science Foundation (RSF) [18-74-10102, 16-14-00052p]; Air Force Office of Scientific ResearchUnited States Department of DefenseAir Force Office of Scientific Research (AFOSR) [FA9550-18-1-0017]
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2019. - Vol. 116, Is. 38. - С. 18911-18916. - ISSN 0027-8424, DOI 10.1073/pnas.1902095116
Примечания : Cited References:16. - We thank the late Dr. Shoji Inoue and Dr. Hisae Kakoi (Meijo University) for providing Odontosyllis materials, Sergey Shakhov for photography, and Drs. Mikhail Baranov and Andrey Mikhaylov for discussions. Some experiments were carried out using equipment provided by the Institute of Bioorganic Chemistry of the Russian Academy of Sciences.ore Facility. Some experiments were supported by Planta LLC. Structural and mechanistic studies were supported by Russian Science Foundation Grant 18-74-10102. Isolation, purification, and biochemical studies were supported by Russian Science Foundation Grant 16-14-00052p. B.R.B. acknowledges support from the Air Force Office of Scientific Research (FA9550-18-1-0017).
Предметные рубрики: MECHANISM
DECARBOXYLATION
OXIDATION
Аннотация: Marine polychaetes Odontosyllis undecimdonta, commonly known as fireworms, emit bright blue-green bioluminescence. Until the recent identification of the Odontosyllis luciferase enzyme, little progress had been made toward characterizing the key components of this bioluminescence system. Here we present the biomolecular mechanisms of enzymatic (leading to light emission) and nonenzymatic (dark) oxidation pathways of newly described O. undecimdonta luciferin. Spectral studies, including 1D and 2D NMR spectroscopy, mass spectrometry, and X-ray diffraction, of isolated substances allowed us to characterize the luciferin as an unusual tricyclic sulfur-containing heterocycle. Odontosyllis luciferin does not share structural similarity with any other known luciferins. The structures of the Odontosyllis bioluminescent system's low molecular weight components have enabled us to propose chemical transformation pathways for the enzymatic and nonspecific oxidation of luciferin.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya, Olga, Ronzhin, Nikita, Posokhina, Ekaterina, Bondar, Vladimir
Заглавие : Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications
Колич.характеристики :10 с
Коллективы : [0356-2019-0022]
Место публикации : Protein J.: SPRINGER, 2021. - Article in press. - ISSN 1572-3887, DOI 10.1007/s10930-021-10010-z. - ISSN 1573-4943(eISSN)
Примечания : Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, Project No. 0356-2019-0022.
Предметные рубрики: ARYL-ALCOHOL OXIDASE
GLUCOSE-OXIDASE
PEROXIDASES
MECHANISM
Аннотация: The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with beta-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H2O2, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55-70 degrees C and pH 5.0. Kinetic parameters K-m and V-max of the oxidase for phenol were 0.21 mM and 0.40 mu M min(-1). We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.
WOS
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chen, Shu-Feng, Vysotski, Eugene S., Liu, Ya-Jun
Заглавие : H2O-Bridged Proton-Transfer Channel in Emitter Species Formation in Obelin Bioluminescence
Колич.характеристики :7 с
Коллективы : Program of Shanghai Institute of Technology [YJ2016-42]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21973005, 21911530094]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085, 19-14-53004]
Место публикации : J. Phys. Chem. B: AMER CHEMICAL SOC, 2021. - Vol. 125, Is. 37. - С. 10452-10458. - ISSN 1520-6106, DOI 10.1021/acs.jpcb.1c03985. - ISSN 1520-5207(eISSN)
Примечания : Cited References:50. - This work was supported by the Program of Shanghai Institute of Technology (no. YJ2016-42), the National Natural Science Foundation of China (21973005 and 21911530094), and the Russian Foundation for Basic Research (20-04-00085 and 19-14-53004).
Предметные рубрики: CHEMILUMINESCENT DECOMPOSITION
FLUORESCENCE-SPECTRA
MECHANISM
QM/MM
Аннотация: Bioluminescence of a number of marine organisms is conditioned by Ca2+-regulated photoprotein (CaRP) with coelenterazine as the reaction substrate. The reaction product, coelenteramide, at the first singlet excited state (S-1) is the emitter of CaRP. The S-1-state coelenteramide is produced via the decomposition of coelenterazine dioxetanone. Experiments suggested that the neutral S-1-coelenteramide is the primary emitter species. This supposition contradicts with theoretical calculations showing that the anionic S-1-coelenteramide is a primary product of the decomposition of coelenterazine dioxetanone. In this study, applying molecular dynamic (MD) simulations and the hybrid quantum mechanics/molecular mechanics (QM/MM) method, we investigated a proton-transfer (PT) process taking place in CaRP obelin from Obelia longissima for emitter formation. Our calculations demonstrate a concerted PT process with a water molecule as a bridge between anionic S-1-coelenteramide and the nearest histidine residue. The low activation barrier as well as the strong hydrogen-bond network between the proton donor and the proton acceptor suggests a fast PT process comparable with that of the lifetime of excited anionic S-1-coelenteramide. The existence of the PT process eliminates the discrepancy between experimental and theoretical studies. The fast PT process at emitter formation can also take place in other CaRPs.
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