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Autotrophic synthesis of polyhydroxyalkanoates by the bacteria Ralstonia eutropha in the presence of carbon monoxide / T. G. Volova, G. S. Kalacheva, O. V. Altukhova // Applied Microbiology and Biotechnology. - 2002. - Vol. 58, Is. 5. - P675-678, DOI 10.1007/s00253-002-0941-8 . - ISSN 0175-7598
Кл.слова (ненормированные):
3 hydroxybutyric acid -- acetoacetyl coenzyme a reductase -- acetyl coenzyme A acyltransferase -- beta hydroxyvalerate -- butyrate dehydrogenase -- carbon monoxide -- electrolyte -- hydrogen -- oxidoreductase -- poly(3 hydroxybutyric acid) -- poly(3 hydroxybutyric acid)synthase -- polyhydroxyalkanoic acid -- polymer -- unclassified drug -- valeric acid -- bacterium -- article -- autotrophy -- bacterial growth -- bacterial strain -- biomass production -- controlled study -- crystallization -- enzyme activity -- molecular weight -- nonhuman -- synthesis -- temperature -- Wautersia eutropha -- Carbon Monoxide -- Culture Media -- Cupriavidus necator -- Fatty Acids -- Lipids -- Polyesters -- Bacteria (microorganisms) -- Negibacteria -- Ralstonia -- Wautersia eutropha
Аннотация: It has been found that the carbon monoxide (CO)-resistant strain of the hydrogen bacteria Ralstonia eutropha B5786 is able to synthesise polyhydroxy-alkanoates (PHAs) in the presence of CO under autotrophic conditions. This strain, grown on model gas mixtures containing 5-25% CO (v/v), accumulates up to 70-75% (of absolutely dry matter) PHA, without significant variation in the yield coefficient on hydrogen. No suppression of the activities of the key enzymes of PHA synthesis (?-ketothiolase, acetoacetyl-CoA-reductase, butyrate dehydrogenase and poly-3-hydroxybutyrate synthase) was recorded. The PHA synthesised is a copolymer containing mostly ?-hydroxybutyrate (more than 99 mol%) with trace amounts of ?-hydroxyvalerate. The investigated properties of the polymer (molecular weight, crystallinity, temperature characteristics) do not differ from those of the polymer synthesised on electrolytic hydrogen.

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

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Altukhova, O.V.

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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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Oxidative stress monitoring in biological samples by bioluminescent method / N. N. Remmel, N. M. Titova, V. A. Kratasyuk // Bulletin of Experimental Biology and Medicine. - 2003. - Vol. 136, Is. 2. - P. 209-211, DOI 10.1023/A:1026347830283 . - ISSN 0007-4888
Кл.слова (ненормированные):
Bioluminescent analysis -- Lipid peroxidation -- Malonic dialdehyde -- Oxidative stress -- malonaldehyde -- animal tissue -- article -- bioluminescence -- brain tissue -- controlled study -- fluorescence -- freeze drying -- kidney parenchyma -- lipid peroxidation -- liver -- male -- monitoring -- nonhuman -- oxidative stress -- Photobacterium phosphoreum -- rat -- serum -- Animals -- Bacteria -- Biological Assay -- Lipid Peroxidation -- Luminescent Measurements -- Malondialdehyde -- Oxidative Stress -- Photobacterium -- Rats -- Tissue Extracts -- Animalia -- Negibacteria -- Photobacterium -- Photobacterium phosphoreum
Аннотация: The integral bioluminescent biotest with lyophilized fluorescent bacteria was used for monitoring of LPO processes in tissue extracts and serum of rats exposed to stress. A relationship between the content of MDA (LPO indicator) and fluorescence of bacteria was observed in all biological samples.

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

Доп.точки доступа:
Remmel, N.N.; Titova, N.M.; Kratasyuk, V.A.

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