Literatura científica selecionada sobre o tema "Rhodopseudomonas"
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Artigos de revistas sobre o assunto "Rhodopseudomonas"
Ramana, V. Venkata, S. Kalyana Chakravarthy, P. Shalem Raj, B. Vinay Kumar, E. Shobha, E. V. V. Ramaprasad, Ch Sasikala e Ch V. Ramana. "Descriptions of Rhodopseudomonas parapalustris sp. nov., Rhodopseudomonas harwoodiae sp. nov. and Rhodopseudomonas pseudopalustris sp. nov., and emended description of Rhodopseudomonas palustris". International Journal of Systematic and Evolutionary Microbiology 62, Pt_8 (1 de agosto de 2012): 1790–98. http://dx.doi.org/10.1099/ijs.0.026815-0.
Texto completo da fonteHarwood, Caroline S. "Rhodopseudomonas palustris". Trends in Microbiology 30, n.º 3 (março de 2022): 307–8. http://dx.doi.org/10.1016/j.tim.2021.12.001.
Texto completo da fonteHuang, Xuejiao, Jiupai Ni, Chong Yang, Mi Feng, Zhenlun Li e Deti Xie. "Efficient Ammonium Removal by Bacteria Rhodopseudomonas Isolated from Natural Landscape Water: China Case Study". Water 10, n.º 8 (20 de agosto de 2018): 1107. http://dx.doi.org/10.3390/w10081107.
Texto completo da fonteXu, Cheng Bin, Xue Kai Sun, Yao Yao Li, Yan Gang Wang e Xue Lian Meng. "Study on Optimization of the Culture Conditions for Four Rhodopseudomonas spp." Advanced Materials Research 393-395 (novembro de 2011): 976–79. http://dx.doi.org/10.4028/www.scientific.net/amr.393-395.976.
Texto completo da fonteHumphrey, Christine E., Nicole Burnett, Shivangi Dubey e John A. Kyndt. "Genomic and Phylogenetic Characterization of Rhodopseudomonas infernalis sp. nov., Isolated from the Hell Creek Watershed (Nebraska)". Microorganisms 10, n.º 10 (13 de outubro de 2022): 2024. http://dx.doi.org/10.3390/microorganisms10102024.
Texto completo da fonteKumar, B. Vinay, E. V. V. Ramprasad, Ch Sasikala e Ch V. Ramana. "Rhodopseudomonas pentothenatexigens sp. nov. and Rhodopseudomonas thermotolerans sp. nov., isolated from paddy soils". International Journal of Systematic and Evolutionary Microbiology 63, Pt_1 (1 de janeiro de 2013): 200–207. http://dx.doi.org/10.1099/ijs.0.038620-0.
Texto completo da fonteZhang, Dong Chen, Zhi Xiang Hou e Tao Wang. "Study on Rhodopseudomonas Spheroides as Coal Microbial Flocculant". Advanced Materials Research 550-553 (julho de 2012): 1090–93. http://dx.doi.org/10.4028/www.scientific.net/amr.550-553.1090.
Texto completo da fonteHiraishi, A., T. S. Santos, J. Sugiyama e K. Komagata. "Rhodopseudomonas rutila Is a Later Subjective Synonym of Rhodopseudomonas palustris". International Journal of Systematic Bacteriology 42, n.º 1 (1 de janeiro de 1992): 186–88. http://dx.doi.org/10.1099/00207713-42-1-186.
Texto completo da fonteImhoff, Johannes F., Terrance E. Meyer e John Kyndt. "Genomic and genetic sequence information of strains assigned to the genus Rhodopseudomonas reveal the great heterogeneity of the group and identify strain Rhodopseudomonas palustris DSM 123T as the authentic type strain of this species". International Journal of Systematic and Evolutionary Microbiology 70, n.º 6 (1 de junho de 2020): 3932–38. http://dx.doi.org/10.1099/ijsem.0.004077.
Texto completo da fonteCampbell, J. I. A., S. Scahill, T. Gibson e R. P. Ambler. "The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A β-lactamase". Biochemical Journal 260, n.º 3 (15 de junho de 1989): 803–12. http://dx.doi.org/10.1042/bj2600803.
Texto completo da fonteTeses / dissertações sobre o assunto "Rhodopseudomonas"
Evans, Katie. "Biochemical characterisation of bacteriophytochromes from Rhodopseudomonas palustris". Thesis, Liverpool John Moores University, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.431289.
Texto completo da fonteMiller, Anthony Raymond Miller. "Investigation of Sulfur Salvage Pathways in Rhodopseudomonas palustris". The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1511908420156965.
Texto completo da fonteEmery, Vincent Clive. "Mechanistic aspects of bacteriochlorophyll A biosynthesis in Rhodopseudomonas sphaeroides". Thesis, University of Southampton, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259664.
Texto completo da fonteVuillet, Laurie. "Caractérisation des bactériophytochromes identifiés chez Rhodopseudomonas palustris et bradyrhizobium". Montpellier 2, 2007. http://www.theses.fr/2007MON20207.
Texto completo da fonteRhodopseudomonas palustris is a photosynthetic purple bacteria which genome was completely sequenced. Six genes encoding putative bactériophytochromes are present in this genome. One of them plays an essential and unusual role in the synthesis of the photosystem. In this bacteria, three other bacteriophytochromes are localized near pucBA operons encoding polypeptides involved in the formation of light harvesting complexes associated with photosystem. First, this PhD work studied roles, properties and mechanisms of action of these three bacteriophytochromes. We showed that RpBphP2 and RpBphP3 act in tandem to regulate the expression of LH4 antennas. This signalling pathway use three reponse-regulators, one of them, Rpa3018 is rdox sensitive. In some strains of Rps. Palustris, a bactériophytochrome, RpBphP4, lost its light sensitivity and acquired a redox sensibility while keeping its ability to regulate the expression of these antennas. In a second time, analysis of the genome sequence of two photosynthetic Bradyrhizobium (ORS278 and BTAi1) revealed, in each strain, the presence of a specific bacteriophytochrome probably acquired by horizontal transfer. The properties of these various bacteriophytochromes led highlighted the variety of this family of light sensors as well as the complexity of the signalling pathways which they introduce
Laing, Ruth Mary Louise. "Development of Rhodopseudomonas palustris as a chassis for biotechnological applications". Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/283194.
Texto completo da fontePott, Robert William McClelland. "The bioconversion of waste glycerol into hydrogen by Rhodopseudomonas palustris". Thesis, University of Cambridge, 2014. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708006.
Texto completo da fonteKamal, Varsha Subhash Carleton University Dissertation Biology. "The anaerobic, phototrophic metabolism of 3-chlorobenzoate by Rhodopseudomonas Palustris". Ottawa, 1992.
Encontre o texto completo da fonteMeckenstock, Udo Rainer. "Isolierung, Charakterisierung und Strukturanalyse des lichtsammelnden B880-Antennenkomplexes von Rhodopseudomonas marina /". [S.l.] : [s.n.], 1993. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=10404.
Texto completo da fonteSalmon, Robert. "The transport and degradation of lignin-derived aromatic compounds by Rhodopseudomonas palustris". Thesis, University of Sheffield, 2014. http://etheses.whiterose.ac.uk/7701/.
Texto completo da fonteGARAU, GIANPIERO. "CRYSTALLOGRAPHIC STUDIES OF METALLOPROTEINS: CYTOCHROME C2 FROM RHODOPSEUDOMONAS PALUSTRIS AND MAMMALIAN TRANSCOBALAMIN". Doctoral thesis, Università degli studi di Trieste, 2003. http://thesis2.sba.units.it/store/handle/item/12657.
Texto completo da fonteThis thesis mainly direct to a few transporter metalloproteins, in particular those containing metallo-organic prosthetic groups (the iron porphyrin and the cobalt corrin complexes ). The three-dimensional structures of the native cytochrome c2 from Rhodopseudomonas palustris and of its ammonia complex have been obtained at pH 4.4 and pH 8.5, respectively. The structure of the native form has been refined in the oxidised state at 1.70 À and in the reduced state at 1.95 À resolution. These are the first highresolution crystal structures in both oxidation states of a cytochrome c2 with relatively high redox potential (+365 mV). The differences between the two oxidation states of the native form, including the position of internal water molecules, are small. The positional change of a buried water molecule, located at the heme binding pocket near to the iron bonded Met, is the most prominent structural difference observed with the change of the iron oxidation state in the c-type cytochrome structures. In all oxidised forms this water molecule is found in a position different from that found in the reduced forms. On the contrary, in the oxidised form of the cytochrome c2 from Rhodopseudomonas palustris, this water molecule is detected in a position close to that found in the reduced form. The buried water molecule plays an important role in adjusting the midpoint redox potential of c-type cytochromes with alteration of the surrounding hydrogen bond network. The unusual six-residue insertion Gly82-Ala87, which precedes the heme binding Met93, forms an isolated 310-helix secondary structural element not previously observed in other c-type cytochromes. Furthermore, this cytochrome shows an extemal methionine residue involved in a strained folding near the exposed edge of the heme. The structural comparison of the present cytochrome c2 with other c-type cytochromes has revealed that the presence of such a residue, with torsion angles and 'V of about -140 and -130°, respectively, is a typical feature of this family of proteins. The refined crystal structure of the ammonia complex, obtained at 1.15 À resolution, shows that the sulphur atom of the Met93 axial ligand does not coordinate the heme iron-atom, but is replaced by an exogenous ammonia molecule. This is the only example so far reported of an X-ray structure with the heme iron coordinated by an ammonia molecule. The detachment of Met93 is accompanied by a very localised change in the backbone conformation, involving mainly the residues Lys92, Met93 and Thr94. Previous studies under typical denaturing conditions, including high pH values and the presence of exogenous ligands, have showed that the detachment of the Met axial ligand is a basic step in the folding/unfolding process of c-type cytochromes. The ammonia-adduct represents a structural model for this important step of the unfolding pathway. Factors proposed to be important for the methionine dissociation are the strength of the H-bond between the Met93 and Tyr66 residues that stabilises the nati ve form, and the presence, in this bacterial cytochrome c2 of the rare six-residue insertion in the helix 310 conformation that increases the Met loop flexibility. Transcobalamin is a cobalamin binding protein in mammalian plasma that facilitates the cellular uptake of vitamin B 12 • Whereas the X-ray structures of severa! B12-enzymes are available, no structural information on B12-transporting proteins has so far been reported. Human and bovine transcobalamin were expressed using ricombinant yeast cells and purified. Human transcobalamin was successfully crystallised usmg polyethylene glycol and ethanol as precipitants. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a= 49.04, b = 145.27, and e= 164.96 À. A complete data set to 3.2 À resolution was collected from a single crystal using s ynchrotron radiati on (Elettra, Trieste). Estimati on of the crystal packing (V m = 3.2 À 3 Da-1) and self-rotation function analysis suggest the presence of two molecules in the asymmetric unit related by a pseudo-twofold symmetry. Bovine transcobalamin was crystallised using polyethylene glycol and MPD. Crystals belong to the monoclinic space group P21 (a = 95.32, b = 100.19, e = 98.73 À and ~ = 96.9 À), and diffract to better then 2.0 À resolution. MAD data sets were collected at Elettra (Trieste) from a single crystal of the bovine protein, using the cobalamin Co atom as anomalous scatterer. Attempts to find the position of Co atoms in the monoclinic cell from Bijvoet difference Patterson maps are under way.
XV Ciclo
1973
Versione digitalizzata della tesi di dottorato cartacea.
Livros sobre o assunto "Rhodopseudomonas"
Lang, Fridl Sebastian. Molekularbiologische Charakterisierung des photosynthetischen Elektronenzyklus in Rhodopseudomonas viridis. Gauting bei München: Intemann, 1988.
Encontre o texto completo da fonteMyatt, John Frederick. Mechanisms of energy coupling in Rhodopseudomonas capsulata. Birmingham: University of Birmingham, 1986.
Encontre o texto completo da fonteLolkema, Julius Sjieuwke. The phosphoenolpyruvate dependent fructose specific phosphotransferase system in Rhodopseudomonas sphaeroides. [s.l.]: [s.n.], 1986.
Encontre o texto completo da fonteWeyer, Karl Aloys. Isolierung und Sequenzierung der Proteinuntereinheiten des photosynthetischen Reaktionszentrums von Rhodopseudomonas viridis: Entdeckung und Strukturaufklärung des Lipoprotein-Membranankers der Cytochrom-Untereinheit. Gauting bei München: Intemann, 1987.
Encontre o texto completo da fonteBreisgau, Universität Freiburg im, ed. Analyse der Poreneigenschaften des Porins aus Rhodopseudomonas blastica durch gezielte Mutagenese, Einzelkanalmessungen und Röntgenstrukturanalyse. [s.l.]: [s.n.], 1997.
Encontre o texto completo da fonteGorham, Hazel C. Characterisation of a novel bacteriophage, 0BHG1: And its interactions with its host "Rhodopseudomonas blastica". [s.l.]: typescript, 1987.
Encontre o texto completo da fonteJohann, Deisenhofer, ed. Structure of the protein subunits in the photosynthetic reaction centre of 'Rhodopseudomonas viridis' at 3A resolution. London: Macmillan Journals, 1985.
Encontre o texto completo da fonteKleemann, Gisela. Hopanoidgehalt und Fettsäuremuster zweier Rhodopseudomonas-Arten und Reinigung der Squalen-Hopen-Cyclase aus Rhodopseudomonas palustris. Tübingen, 1992.
Encontre o texto completo da fonteMorrison, Linda Carol. Localization of the NIF genes in Rhodopseudomonas gelatinosa. 1986.
Encontre o texto completo da fonteLancaster, C. Roy D. The coupling of light-induced electron transfer to proton uptake in the photosynthetic reaction centre from Rhodopseudomonas viridis. 1996.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Rhodopseudomonas"
Dow, C. S. "CO2 Fixation in Rhodopseudomonas Blastica". In Microbial Growth on C1 Compounds, 28–37. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3539-6_4.
Texto completo da fonteKnobloch, Karl, Birigt Pirner e Horst Müller. "Membrane Properties of Rhodopseudomonas palustris". In Current Research in Photosynthesis, 2091–94. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_480.
Texto completo da fonteEvans, Katie, Toni Georgiou, Theresa Hillon, Anthony Fordham-Skelton e Miroslav Papiz. "Bacteriophytochromes Control Photosynthesis in Rhodopseudomonas palustris". In The Purple Phototrophic Bacteria, 799–809. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-1-4020-8815-5_40.
Texto completo da fonteBittersmann, Edith, Robert E. Blankenship e Neal Woodbury. "Picosecond Fluorescence Studies of Rhodopseudomonas viridis". In Current Research in Photosynthesis, 1129–32. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_262.
Texto completo da fonteVrieze, J., e A. J. Hoff. "Exciton Band Mixing in Rhodopseudomonas viridis". In Reaction Centers of Photosynthetic Bacteria, 409–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-61297-8_40.
Texto completo da fonteBerry, Edward A., e Antony R. Crofts. "Cytochrome Oxidase of Photosynthetically Grown Rhodopseudomonas Sphaeroides". In Progress in Photosynthesis Research, 661–64. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_157.
Texto completo da fonteKnobloch, Karl, Helmut Vigenschow e Hans-Martin Schwarm. "Phosphotransacetylase and Acetate Kinase from Rhodopseudomonas Palustris". In Progress in Photosynthesis Research, 229–32. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-017-0516-5_49.
Texto completo da fonteShopes, R. J., e C. A. Wraight. "Herbicide-Resistant Reaction Center Mutants of Rhodopseudomonas Viridis". In Progress in Photosynthesis Research, 397–400. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_95.
Texto completo da fonteBarrett, S. J., e R. J. Cogdell. "Investigation of the PucC Protein from Rhodopseudomonas acidophila". In Photosynthesis: Mechanisms and Effects, 3091–94. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_723.
Texto completo da fonteHara, Masayuki, Christopher C. Moser e P. Leslie Dutton. "Electrochromic Band-Shift of Carotenoid in Rhodopseudomonas Viridis". In Photosynthesis: from Light to Biosphere, 555–58. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_129.
Texto completo da fonteTrabalhos de conferências sobre o assunto "Rhodopseudomonas"
Dong, Yi-Hua, Peng Li, Jiang-Hai He, Shu-Yuan Zhang e Liang Li. "Degradation of O-chlorophenol BY Rhodopseudomonas sp. PSB-1D". In 2015 International Conference on Energy, Environmental & Sustainable Ecosystem Development (EESED 2015). WORLD SCIENTIFIC, 2015. http://dx.doi.org/10.1142/9789814723008_0044.
Texto completo da fonteZinth, W., M. C. Nuss e W. Kaiser. "Femtosecond Studies of Bacterial Photosynthesis". In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.wa2.
Texto completo da fonteMatveets, Yu A., S. V. Chekalin e A. P. Yartsev. "Femtosecond-Pulse Spectroscopy of Primary Photoprocesses in Reaction Centers of Rhodopseudomonas Sphaeroides R-26". In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.mf6.
Texto completo da fonteKlug, David R., James R. Durrant, Gary Hastings, Qiang Hong, James Barber e George Porter. "Primary charge separation in Photosystem Two Reaction Centres". In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.wa4.
Texto completo da fonteYihua, Dong, Hu Xiaomin, He Yingdian e Li Liang. "Biodegradation of O-chlorophenol by Rhodopseudomonas palustris PSB-1D and Optimization of Cometabolism Substrates". In 2011 International Conference on Computer Distributed Control and Intelligent Environmental Monitoring (CDCIEM). IEEE, 2011. http://dx.doi.org/10.1109/cdciem.2011.441.
Texto completo da fonteZhao, Xiao-Hui, Rong-Xiang Zhang, Xiao-Dong Tian, Guang Li, Lian-Shui Zhang e Xiao-Ting Li. "Singlet-Excitation Energy Transfer Among Carotenoids in the HL-LH2 Complex from Rhodopseudomonas Palustris". In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.314.
Texto completo da fonteFan, Zhiping, Fayun Li, Xuekai Sun e Hongshuang Jing. "Notice of Retraction: Effects of Cultivation Conditions on Growth of Rhodopseudomonas palustris Isolated from Aquaculture Wastewater". In 2011 5th International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2011. http://dx.doi.org/10.1109/icbbe.2011.5781089.
Texto completo da fonteMartin, J. L., J. Breton, J. C. Lambry, M. E. Michel-Beyerle, R. Feick, S. R. Robles e D. Youvan. "Primary Charge Separation Process in Reaction Centers". In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1990. http://dx.doi.org/10.1364/up.1990.mb2.
Texto completo da fonteBESSA, L. P., L. M. VIEIRA, F. T. M. SILVA, J. S. FERREIRA, L. C. VICELMA e F. R. X. BATISTA. "DETERMINAÇÃO DA BACTERIOCLOROFILA E DA CONCENTRAÇÃO CELULAR DAS BACTÉRIAS PÚRPURAS NÃO SULFUROSAS Rhodobacter capsulatus e Rhodopseudomonas palustris". In XI Congresso Brasileiro de Engenharia Química em Iniciação Científica. São Paulo: Editora Edgard Blücher, 2015. http://dx.doi.org/10.5151/chemeng-cobeqic2015-245-32992-262770.
Texto completo da fonte"Thermodynamics of Biosorption of Zn and Cu in Aqueous Solution by Rhodopseudomonas boonkerdii sp. strain NS20 and Bradyrhizobium sp. strain DOA9". In International Conference on Advances in Engineering and Technology. International Institute of Engineers, 2014. http://dx.doi.org/10.15242/iie.e0314161.
Texto completo da fonteRelatórios de organizações sobre o assunto "Rhodopseudomonas"
Harwood, Caroline S. Rhodopseudomonas palustris genome project. Final report. Office of Scientific and Technical Information (OSTI), novembro de 2000. http://dx.doi.org/10.2172/807067.
Texto completo da fonteHarwood, Caroline S. Final report: 'Rhodopseudomonas palustris' genome workshop to be held in Spring of 2001. Office of Scientific and Technical Information (OSTI), junho de 2002. http://dx.doi.org/10.2172/771267.
Texto completo da fonte(Organization and regulation of the genes for nitrogen fixation in Rhodopseudomonas capsulata). Office of Scientific and Technical Information (OSTI), janeiro de 1991. http://dx.doi.org/10.2172/7066453.
Texto completo da fonte[Organization and regulation of the genes for nitrogen fixation in Rhodopseudomonas capsulata]. Progress report, [June 5, 1989--June 4, 1991]. Office of Scientific and Technical Information (OSTI), dezembro de 1991. http://dx.doi.org/10.2172/10166528.
Texto completo da fonte