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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Natashin P.V., Song L..., Zhou Y.G., van Berkel WJH, Liu Z.J., Vysotski E.S.
Заглавие : Oxygen Activation of Apo-obelin-Coelenterazine Complex
Колич.характеристики :7 с
Место публикации : ChemBioChem: WILEY-V C H VERLAG GMBH, 2013. - Vol. 14, Is. 6. - С. 739-745. - ISSN 1439-4227, DOI 10.1002/cbic.201300002
Примечания : Cited References: 46. - The work was supported by grants from the RFBR 12-04-91153, and NSFC 31270795 and 31021062, by the Russian Federation Government Program "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of the Russian Federation "Leading Science School" (grant 1044.2012.2). E.V.E. was supported by a Wageningen University Sandwich PhD Fellowship Program.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
JELLYFISH CLYTIA-GREGARIA
CRYSTAL-STRUCTURE
CA2+-DISCHARGED PHOTOPROTEIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
MOLECULAR-OXYGEN
AEQUORIN
CALCIUM
BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): aequorin--coelenterazine--luminescence--photoprotein--protein folding
Аннотация: Ca2+-regulated photoproteins use a noncovalently bound 2-hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo-obelincoelenterazine complex and the kinetics of its conversion into active photoprotein after exposure to air. Our studies suggest that coelenterazine bound within the anaerobic complex might be a mixture of N7-protonated and C2() anionic forms, and that oxygen shifts the equilibrium in favor of the C2() anion as a result of peroxy anion formation. Proton removal from N7 and further protonation of peroxy anion and the resulting formation of 2-hydroperoxycoelenterazine in obelin might occur with the assistance of His175. It is proposed that this conserved His residue might play a key role both in formation of active photoprotein and in Ca2+-triggering of the bioluminescence reaction.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Titushin M.S., Markova S.V., Frank L.A., Malikova N.P., Stepanyuk G.A., Lee J..., Vysotski E.S.
Заглавие : Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase
Колич.характеристики :8 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2008. - Vol. 7, Is. 2. - С. 189-196. - ISSN 1474-905X, DOI 10.1039/b713109g
Примечания : Cited References: 41
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Liu Z.J., Markova S.V., Blinks J.R., Deng L..., Frank L.A., Herko M..., Malikova N.P., Rose J.P., Wang B.C., Lee J...
Заглавие : Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species
Колич.характеристики :12 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2003. - Vol. 42, Is. 20. - С. 6013-6024. - ISSN 0006-2960, DOI 10.1021/bi027258h
Примечания : Cited References: 45
Предметные рубрики: RAY CRYSTALLOGRAPHIC ANALYSIS
PHOTOPROTEIN AEQUORIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CALCIUM
LUMINESCENCE
LONGISSIMA
EVOLUTION
PROTEINS
COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Westphal A.H., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding
Колич.характеристики :6 с
Коллективы : Wageningen University Sandwich PhD-Fellowship Program [02.512.12. 2006]; Ministry of Education and Science of Russian Federation, MCB Program of RAS [1211.2008.4]; SB RAS
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2009. - Vol. 583, Is. 12. - С. 1939-1944. - ISSN 0014-5793, DOI 10.1016/j.febslet.2009.04.043
Примечания : Cited References: 28. - We thank Prof. John Lee for valuable suggestions and providing constructive criticisms. The work was supported by Wageningen University Sandwich PhD-Fellowship Program, Grants 02.512.12. 2006 and 1211.2008.4 of Ministry of Education and Science of Russian Federation, MCB Program of RAS, and by Grant No. 2 of SB RAS.
Предметные рубрики: CRYSTAL-STRUCTURE
CA2+-REGULATED PHOTOPROTEINS
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
W92F OBELIN
CALCIUM
REGENERATION
APOAEQUORIN
EXPRESSION
Ключевые слова (''Своб.индексиров.''): bioluminescence--photoprotein--trp fluorescence
Аннотация: The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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