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The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - P774-779, DOI 10.1006/bbrc.1995.1880 . - ISSN 0006-291X
Кл.слова (ненормированные):
riboflavin -- article -- bioluminescence -- fluorescence -- nonhuman -- priority journal -- protein analysis -- protein synthesis -- vibrio -- vibrionaceae -- Bacterial Proteins -- Chromatography, Gel -- Chromatography, Thin Layer -- Flavin Mononucleotide -- Flavoproteins -- Luminescence -- Riboflavin -- Spectrometry, Fluorescence -- Support, U.S. Gov't, P.H.S. -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Vibrio -- Vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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Isolation and comparative study of two fluorescent flavoproteins of the luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biophysics. - 1990. - Vol. 35, Is. 2. - P377-379 . - ISSN 0006-3509

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:
Raibekas, A.A.; Petushkov, V.N.

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Isolation and comparative studies of two fluorescent flavoproteins of luminous bacteria Photobacterium leiognathi / A. A. Raibekas, V. N. Petushkov // Biofizika. - 1990. - Vol. 35, Is. 2. - С. 368-370 . - ISSN 0006-3029
Кл.слова (ненормированные):
flavoprotein -- fluorescence -- letter -- nonhuman -- Photobacterium leiognathi

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

Доп.точки доступа:
Raibekas, A.A.; Petushkov, V.N.

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Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

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

Доп.точки доступа:
Raibekas, A.A.

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