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The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems / V. A. Kratasyuk [et al.] // Chemosphere. - 2001. - Vol. 42, Is. 8. - P909-915, DOI 10.1016/S0045-6535(00)00177-6 . - ISSN 0045-6535
Кл.слова (ненормированные):
Alcohol dehydrogenase -- Bacterial luciferase -- Bioluminescence -- Blooming -- Pollution -- Trypsin -- Water toxicity -- alcohol dehydrogenase -- benzoquinone -- luciferase -- trypsin -- aquatic ecosystem -- bioluminescence -- water quality -- article -- bacterium culture -- bioluminescence -- blue green alga -- ecosystem -- pond -- seasonal variation -- water pollution -- water quality -- Benzoquinones -- Biological Assay -- Cyanobacteria -- Ecosystem -- Environmental Monitoring -- Eutrophication -- FMN Reductase -- Indicators and Reagents -- Luminescent Measurements -- NADH, NADPH Oxidoreductases -- Water Pollutants -- Russian Federation -- algae -- Bacteria (microorganisms) -- Chlorophyta -- Cyanobacteria -- uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.

Scopus
Держатели документа:
Krasnoyarsk State University, pr. Svobodnii 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Esimbekova, E.N.; Gladyshev, M.I.; Khromichek, E.B.; Kuznetsov, A.M.; Ivanova, E.A.

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Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another / N. S. Rodionova, V. N. Petushkov, P. I. Belobrov // Biophysics. - 1988. - Vol. 33, Is. 3. - P424-430 . - ISSN 0006-3509
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.

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

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

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Nucleotide sequence of part of Photobacterium leiognathi lux region / B. A. Illarionov [et al.] // Nucleic Acids Research. - 1988. - Vol. 16, Is. 20. - P9855, DOI 10.1093/nar/16.20.9855 . - ISSN 0305-1048
Кл.слова (ненормированные):
bacterial protein -- luciferase -- article -- bacterial gene -- genetics -- molecular genetics -- nucleotide sequence -- Photobacterium -- Bacterial Proteins -- Base Sequence -- Genes, Bacterial -- Luciferase -- Molecular Sequence Data -- Photobacterium

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Krasnoyarsk, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, 630090, Novosibirsk, Lavrentjev prospect 8, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarionov, B.A.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes / B. A. Illarrionov [et al.] // Gene. - 1990. - Vol. 86, Is. 1. - P89-94 . - ISSN 0378-1119
Кл.слова (ненормированные):
Bioluminescence -- expression in E. coli -- luciferase -- molecular evolution -- nucleotide sequence -- protein alignment -- recombinant DNA -- luciferase -- amino acid sequence -- article -- bioluminescence -- fungus -- gene structure -- genetic engineering -- heredity -- nonhuman -- nucleotide sequence -- priority journal -- vibrionaceae -- Acyltransferases -- Amino Acid Sequence -- Bacterial Proteins -- Base Sequence -- Cloning, Molecular -- DNA, Bacterial -- Genes, Structural, Bacterial -- Luciferase -- Luminescence -- Molecular Sequence Data -- Operon -- Photobacterium -- Restriction Mapping -- Escherichia coli -- Fungi -- Photobacterium leiognathi -- Vibrio harveyi -- Vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, 660062, Russian Federation
All-Union Research Institute of Molecular Biology, Novosibirsk Region, 633159, Russian Federation
Institute of Biophysics, Krasnoyarsk, 660036, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, 630090, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarrionov, B.A.; Blinov, V.M.; Douchenko, A.P.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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А.с. 973614 СССР, МКИ C 12 N 9/02.

Высоцкий, Е. С.
Питательная среда для культивирования светящихся бактерий [Текст] / Е. С. Высоцкий, В. В. Заворуев, В. В. Межевикин ; Ин-т биофизики СО АН СССР. - № 3281527 ; Заявл. 29.04.1981 ; Опубл. 15.11.1982. -

ГРНТИ

34.27.51

РУБ 343.27.51
Рубрики:
КУЛЬТИВИРОВАНИЕ КЛЕТОК
   СВЕТЯЩИЕСЯ БАКТЕРИИ
   ПИТАТЕЛЬНАЯ СРЕДА
   ЛЮЦИФЕРАЗА
   БИОСИНТЕЗ
   ПАТЕНТЫ
   BIOTECHNOLOGY
   LUCIFERASE PRODUCTION
   PATENT
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Заворуев, В.В.; Межевикин, В.В.; Ин-т биофизики СО АН СССР
Свободных экз. нет
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^a314.27.17^2VINITI
И 88

Исследование природного флавинового субстрата бактериальной люциферазы [Текст] : научное издание / В. С. Бондарь [и др.] // Докл. АН СССР. - 1987. - Т. 293, N 5. - С. 1253-1255 . - ISSN 0002-3264

ГРНТИ

34.15.21

31.27.17

РУБ 314.27.17 + 343.15.21
Рубрики:
ЛЮЦИФЕРАЗА
   СУБСТРАТЫ ПРИРОДНЫЕ
   ФЛАВОПРОТЕИН
   ПОЛУЧЕНИЕ
   СВОЙСТВА
   БАКТЕРИИ
   LUCIFERASE
   А ОР ОТЕ
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, Владимир Станиславович; Высоцкий, Евгений Степанович; Межевикин, В. В.; Райбекас, А. А.

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^a621.13.41^2VINITI
П 53

Получение препарата бактериальной люциферазы для биолюминесцентного анализа [Текст] : научное издание / В. С. Бондарь [и др.] // Прикл. биохимия и микробиол. - 1988. - Т. 24, N 6. - С. 745-753 . - ISSN 0555-1099

ГРНТИ

62.13.41

РУБ 621.13.41
Рубрики:
ФЕРМЕНТНЫЕ ПРЕПАРАТЫ
   ЛЮЦИФЕРАЗЫ
   PHOTOBACTERIUM LEIOGNATHI
   БИОЛЮМИНЕСЦЕНТНЫЙ АНАЛИЗ
   LUCIFERASE
   ВАСТЕ А
Аннотация: Описано получение препарата бактериальной люциферазы из бактерий Photobacterium leiognathi, предназначенной для определения содержания НАД(Ф)Н и активности НАД(Ф)-зависимых дегидрогеназ. Метод основан на использовании доступных и дешевых адсорбентов и включает только две хроматографические стадии. По данным SDS-фореза бактериальная люцифераза из P. leiognathi состоит из двух субъединиц и имеет молекулярную массу около 88 000. Библ. 24. Ин-т биофизики СО АН СССР, Красноярск, СССР
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Высоцкий, Е.С.; Заворуев, В.В.; Межевикин, В.В.; Райбекас, А.А.

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Growth and luminescence of luminous bacteria promoted by agents of microbial origin. / E. K. Rodicheva [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P293-299 . - ISSN 0884-3996
Кл.слова (ненормированные):
amino acid -- carbohydrate -- folic acid -- luciferase -- nitrogen -- riboflavin -- article -- biosynthesis -- culture medium -- electron microscopy -- growth, development and aging -- kinetics -- luminescence -- metabolism -- Photobacterium -- physiology -- time -- ultrastructure -- Vibrio -- Amino Acids -- Carbohydrates -- Culture Media -- Folic Acid -- Kinetics -- Luciferase -- Luminescence -- Microscopy, Electron -- Nitrogen -- Photobacterium -- Riboflavin -- Time Factors -- Vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.

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

Доп.точки доступа:
Rodicheva, E.K.; Trubachev, I.N.; Medvedeva, S.E.; Egorova, O.I.; , U - Shitova LYu

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The effect of succinic acid sulfoderivatives on bacterial luminescence / V. A. Kratasyuk [и др.] // Prikladnaya Biokhimiya i Mikrobiologiya. - 1991. - Vol. 27, Is. 1. - С. 127-133 . - ISSN 0555-1099
Кл.слова (ненормированные):
luciferase -- n (arylsulfonamido)succinimide -- unclassified drug -- article -- bacterium -- bioluminescence -- nonhuman -- Bacteria (microorganisms)

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch of the USSR Academy of Sciences, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Makurina, V.I.; Kuznetsov, A.M.; Kudryasheva, N.S.; Plotnikova, N.B.; Medvedeva, S.E.; Gritsenko, I.S.; Chernykh, V.P.

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10.

BIOLUMINESCENT ANALYSIS - THE ACTION OF TOXICANTS - PHYSICAL-CHEMICAL REGULARITIES OF THE TOXICANTS EFFECTS [Text] / N. S. KUDRYASHEVA, V. A. KRATASYUK, P. I. BELOBROV // Anal. Lett. - 1994. - Vol. 27, Is. 15. - P2931-2947. - Cited References: 13 . - 17. - ISSN 0003-2719

РУБ Chemistry, Analytical

Кл.слова (ненормированные):
BACTERIAL LUCIFERASE BIOTEST -- FOREIGN COMPOUNDS -- ENERGY OF ELECTRON EXCITED STATES LEVEL -- REDOX POTENTIAL -- REDUCING OF BIOLUMINESCENT INTENSITY -- INDUCTION PERIOD -- TIME OF MAXIMUM LIGHT INTENSITY
Аннотация: The physical-chemical regularities of aromatic compounds' effects in luciferase to toxicity biotesting have been studied, The structures and physical-chemical characteristics of the toxicants and of the bioluminescent emitter were taken into account. The inhibition constants of bioluminescence intensity (I) were calculated and interpreted from the viewpoint of the energy (electron) transfer processes. The induction period (P) and the increase of the rime of the maximum light intensity (t(M)) which take place in the quinones presence, have been shown to deal with hydrogen transfer processes. The values of I, P and t(M) have been shown to be connected with a size of the quinones' aromatic and aliphatic parts, P- and t(M)-dependencies on quinone's redox potential have been demonstrated.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
KUDRYASHEVA, N.S.; KRATASYUK, V.A.; BELOBROV, P.I.

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11.

CONFORMATIONAL RELAXATION OF BACTERIAL LUCIFERASE [Текст] / N. S. RODIONOVA, V. N. PETUSHKOV, P. I. BELOBROV // Biofizika. - 1988. - Vol. 33, Is. 3. - С. 396-400. - Cited References: 10 . - 5. - ISSN 0006-3029

РУБ Biophysics

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
RODIONOVA, N.S.; PETUSHKOV, V.N.; BELOBROV, P.I.

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12.

EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV, N. S. RODIONOVA, P. I. BELOBROV // Biochem.-Moscow. - 1985. - Vol. 50, Is. 3. - P338-342. - Cited References: 13 . - 5. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; RODIONOVA, N.S.; BELOBROV, P.I.

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13.

2-ENZYME NADH-FMN-OXIDOREDUCTASE-LUCIFERASE SYSTEM FROM LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV [et al.] // Biochem.-Moscow. - 1984. - Vol. 49, Is. 4. - P593-603. - Cited References: 24 . - 11. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

Держатели документа:
LV KIRENSKII PHYS INST,KRASNOYARSK,USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; KRATASYUK, G.A.; RODIONOVA, N.S.; FISH, A.M.; BELOBROV, P.I.

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14.

THERMAL INACTIVATION OF BACTERIAL LUCIFERASE [Text] / V. N. PETUSHKOV [et al.] // Biochem.-Moscow. - 1982. - Vol. 47, Is. 11. - P1504-1508. - Cited References: 10 . - 5. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

Держатели документа:
LV KIRENSKII PHYS INST,KRASNOYARSK,USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; KRATASYUK, G.A.; KRATASYUK, V.A.; BELOBROV, P.I.

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15.

INVESTIGATION OF NATIVE FLAVIN SUBSTRATE OF BACTERIAL LUCIFERASE [Текст] / V. S. BONDAR [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1987. - Vol. 293, Is. 5. - С. 1253-1255. - Cited References: 7 . - 3. - ISSN 0002-3264

РУБ Multidisciplinary Sciences

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BONDAR, V.S.; VYSOTSKII, E.S.; MEZHEVIKIN, V.V.; RAIBEKAS, A.A.

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16.

LOCALIZATION OF LUCIFERASE IN THE LUMINOUS BACTERIA PHOTOBACTERIUM-PHOSPHOREUM [Текст] / V. V. MEZHEVIKIN [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1981. - Vol. 258, Is. 6. - С. 1470-&. - Cited References: 9 . - 0. - ISSN 0002-3264

РУБ Multidisciplinary Sciences

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
MEZHEVIKIN, V.V.; VYSOTSKII, E.S.; ZAVORUEV, V.V.; SALNIKOV, M.V.

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17.

REGULATION OF LUCIFERASE SYNTHESIS IN PHOTOBACTERIUM-MANDAPAMENSIS [Text] / T. I. VOROBEVA [et al.] // Microbiology. - 1980. - Vol. 49, Is. 4. - P452-455. - Cited References: 8 . - 4. - ISSN 0026-2617

РУБ Microbiology

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
VOROBEVA, T.I.; VYSOTSKII, E.S.; ZAVORUEV, V.V.; MEZHEVIKIN, V.V.

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18.

A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN [Text] / L. Y. Antipina [et al.] // J. Struct. Chem. - 2011. - Vol. 52, Is. 5. - P870-875. - 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). . - ISSN 0022-4766

РУБ Chemistry, Inorganic & Nuclear + Chemistry, Physical
Рубрики:
CALCIUM-DISCHARGED OBELIN
   SEMIEMPIRICAL METHODS
   1.7 ANGSTROM
   OPTIMIZATION
   PARAMETERS
   MECHANISM
   FLUORESCENCE
   ELEMENTS
   PROTEIN
   EMITTER
Кл.слова (ненормированные):
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.

Держатели документа:
[Antipina, L. Yu
Tomilin, F. N.
Ovchinnikov, S. G.] Russian Acad Sci, LV Kirensky Phys Inst, Siberian Div, Krasnoyarsk, Russia
[Vysotskii, E. S.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Antipina, L. Yu
Ovchinnikov, S. G.] MF Reshetnev Siberian State Aerosp Univ, Krasnoyarsk, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Antipina, L.Y.; Tomilin, F.N.; Vysotskii, E.S.; Ovchinnikov, S.G.

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19.

Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase / E. V. Eremeeva, S. V. Markova, E. S. Vysotski // Dokl. Biochem. Biophys. - 2013. - Vol. 450, Is. 1. - P147-150, DOI 10.1134/S1607672913030095. - Cited References: 14. - This work was supported by the Ministry of Education and Science of the Russian Federation (Government Contract no. 16.512.11.2141) and Council of the President of the Russian Federation on Grants and State Support of Leading Scientific Schools (project no. NSh-64987.2010.4). . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
   GENE-EXPRESSION
   CDNA
   CLONING
   BIOLUMINESCENCE
   RENIFORMIS

Scopus
Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodnyi pr. 79, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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20.

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

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

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

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

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