Results 141 to 150 of about 18,001 (187)

Citramalatosintasa en rhodopseudomonas palustris

, 2017
Cánovas Palacio-Valdés, José Luis, Ruiz-Amil, Manuel, Losada Villasante, Manuel   +2 more
openaire   +2 more sources

Phototrophic Lactate Utilization by Rhodopseudomonas palustris Is Stimulated by Coutilization with Additional Substrates. [PDF]

Appl Environ Microbiol, 2019
Govindaraju A, McKinlay JB, LaSarre B.
europepmc   +1 more source

A genetic tool for production of GFP-expressing Rhodopseudomonas palustris for visualization of bacterial colonization. [PDF]

AMB Express, 2019
Zhai Z, Du J, Chen L, Hamid MR, Du X, Kong X, Cheng J, Tang W, Zhang D, Su P, Liu Y.   +10 more
europepmc   +1 more source

Anaerobic utilization of phenanthrene by Rhodopseudomonas palustris

Biotechnology Letters, 2011
A phenanthrene-utilizing bacterium was anaerobically isolated and identified as Rhodopseudomonas palustris. It tolerated up to 100 mg phenanthrene l(-1) and degraded 50% of 50 mg phenanthrene l(-1) over 10 days. The presence of phenanthrene caused a prolonged lag phase (2-3 days) in cell growth and affected the photopigments biosynthesis, while DMSO ...
Suping Yang, Chungui Zhao, Shaohua Chen   +2 more
exaly   +5 more sources

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, 2020
The genus Rhodopseudomonas , containing purple nonsulfur photosynthetic Proteobacteria, has a number of strains that belong to different species, although many of them are collectively called Rhodopseudomonas palustris . The type species R. palustris and
John Kyndt, Johannes F Imhoff
exaly   +2 more sources

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Porphobilinogenase from Rhodopseudomonas palustris

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1989
1. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the amount of PBG consumed. 3.
A A, Juknat, M L, Kotler, G E, Koopmann, A M, Batlle   +3 more
openaire   +2 more sources

The Photosynthetic Apparatus of Rhodopseudomonas palustris: Structures and Organization

Journal of Molecular Biology, 2006
The structural analysis of the individual components of the photosynthetic apparatus of Rhodopseudomonas palustris, or those of related species, is almost complete. To shed light on the assembly and organization of this machinery, we have studied native membranes of Rps.palustris grown under different light conditions using atomic force microscopy (AFM)
Scheuring, Simon, Pedro Goncalves, Rui, Prima, Valérie, Sturgis, James   +3 more
openaire   +3 more sources

Biodegradation of 2-Chlorophenol byRhodopseudomonas palustris

Bioremediation Journal, 2012
A phototrophic bacterial culture that assimilates 2-chlorophenol (2-CP) was enriched from effluents of paper and wood industry. The isolated bacterium was identified as Rhodopseudomonas palustris based on its morphological characteristics, biochemical ...
Govindareddy, V., Mutharasaiah, K., Chandrakant, K.   +2 more
exaly   +2 more sources

Membrane Properties of Rhodopseudomonas palustris

1990
Among purple bacteria, energy transformation rates are rather low in Rhodopseudomonas palustris (ATCC 11168) due to a weakly membrane-bound RpF1-ATPase. Cell breakage by high pressure or sonication treatment resulted in a crude chromatophore preparation with a lag phase of about 6 h where no energy induced H+ uptake or phosphorylation rate could be ...
Karl Knobloch, Birigt Pirner, Horst Müller   +2 more
openaire   +1 more source

Purification and properties of the adenylate kinases from Rhodopseudomonas palustris, Rhodopseudomonas sphaeroides and Rhodopseudomonas rubrum

Archives of Microbiology, 1983
The adenylate kinases (EC 2.7.4.3) from photosynthetically grown Rhodopseudomonas palustris, Rhodopseudomonas sphaeroides and Rhodospirillum rubrum were purified to homogeneity by the same procedure. The purified enzymes showed optimal rates of activity with MgCl2 at 25° C and pH 8.0.
Hartmut Neufang, Horst M�ller, Karl Knobloch   +2 more
openaire   +1 more source