Disease relevance of Rhodopseudomonas

• The lifetimes of the carotenoid S(1) states in the B800-B850 complex and B800-B820 complex of Rhodopseudomonas acidophila are 7+/-0.5 ps and 6+/-0.5 ps, respectively, and in the light-harvesting complex 2 of Rhodobacter sphaeroides approximately 1.9+/-0.5 ps [1].
• Unlike the diphosphoryl lipid A (DPLA) derived from toxic lipopolysaccharide of Escherichia coli and Salmonella strains, the DPLA from nontoxic lipopolysaccharide of Rhodopseudomonas sphaeroides ATCC 17023 is biologically inactive [2].
• In this work we investigate the origin and characteristics of the circular dichroism (CD) spectrum of rhodopin glucoside and lycopene in the light-harvesting 2 complex of Rhodopseudomonas acidophila and Rhodospirillum molischianum, respectively [3].
• Acetylene reduction by whole cells of Rhodopseudomonas capsulata, Rhodospirillum rubrum, and Chromatium vinosum strain D was inhibited 50% by 0.73, 0.32, and 0.26 microM O2, respectively [4].
• Nitrous oxide reduction by members of the family Rhodospirillaceae and the nitrous oxide reductase of Rhodopseudomonas capsulata [5].

High impact information on Rhodopseudomonas

• Here we report feedback-optimized coherent control over the energy-flow pathways in the light-harvesting antenna complex LH2 from Rhodopseudomonas acidophila, a photosynthetic purple bacterium [6].
• The simulations, based on the crystallographic structure of the reaction center from Rhodopseudomonas viridis, focus on electron transfer from a bacteriopheophytin to a quinone and the subsequent back-reaction [7].
• However, the triazine-resistant mutant T4 from Rhodopseudomonas (Rps.) viridis, which has the tyrosine residue at position 222 on the L subunit substituted for phenylalanine (TyrL222Phe), is sensitive to both ureas and phenolics [8].
• Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration) [9].
• Reduced (Fe(II)) Rhodopseudomonas palustris cytochrome c' (Cyt c') is more stable toward unfolding ([GuHCl](1/2) = 2.9(1) M) than the oxidized (Fe(III)) protein ([GuHCl](1/2) = 1.9(1) M) [10].

Chemical compound and disease context of Rhodopseudomonas

• To determine the molecular basis for this environmentally important process, we cloned and analyzed genes required for the anaerobic degradation of benzoate and related compounds from the phototrophic bacterium, Rhodopseudomonas palustris [11].
• Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate [12].
• Isolation and characterization of the pigment-protein complexes of Rhodopseudomonas sphaeroides by lithium dodecyl sulfate/polyacrylamide gel electrophoresis [13].
• Chemical reduction of 3-oxo and unsaturated groups in fatty acids of diphosphoryl lipid A from the lipopolysaccharide of Rhodopseudomonas sphaeroides. Comparison of biological properties before and after reduction [2].
• Photoaffinity labeling of an antimycin-binding site in Rhodopseudomonas sphaeroides [14].

Biological context of Rhodopseudomonas

• Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides [15].
• In the photosynthetic bacterium Rhodopseudomonas capsulata mutations that affect carotenoid biosynthesis before colored carotenoids are formed have a "blue-green" phenotype as opposed to the "red" of wild type cells [16].
• Kinetics of electron transfer from the bound tetraheme cytochrome c to the primary donor (P) have been measured in isolated reaction centers of the purple bacterium Rhodopseudomonas viridis by time-resolved flash absorption spectroscopy [17].
• Comparison of permeant ion uptake and carotenoid band shift as methods for determining the membrane potential in chromatophores from Rhodopseudomonas sphaeroides Ga [18].
• We look at how sequence variations that would affect the shape of the cardiolipin binding site might affect the protein-cardiolipin interaction, by modeling the binding of cardiolipin to the reaction center from Rhodopseudomonas viridis [19].

Anatomical context of Rhodopseudomonas

• Concentrations for 50% inhibition in chromatophores of Rhodopseudomonas sphaeroides (at 0.4 microM reaction center) are 2 microM for undecyl-, 3 microM for octyl-, and 40 microM for pentyl-substituted hydroxynaphthoquinones [20].
• Inhibition of electron transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome c oxidoreductases of Rhodopseudomonas sphaeroides and mammalian mitochondria. Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster [20].
• The antimycin-sensitive ubisemiquinone radical (QC) of the ubiquinol-cytochrome c oxidoreductase of submitochondrial particles and chromatophores of Rhodopseudomonas sphaeroides Ga has been studied by a combination of redox potentiometry and EPR spectroscopy [21].
• In this work we explain the spectral heterogeneity of the absorption band (. Biochim. Biophys. Acta. 1229:373-380), as well as the spectral evolution of pump-probe spectra for membranes of Rhodopseudomonas (Rps.) viridis [22].
• Inactivation of suppressor T cell activity by the nontoxic lipopolysaccharide of Rhodopseudomonas sphaeroides [23].

Gene context of Rhodopseudomonas

• Addition of monophosphoryl lipid A, but not the threonyl derivative of muramyl dipeptide or nontoxic Rhodopseudomonas sphaeroides lipopolysaccharide, to copolymer L121 increased production of the IgG2a, IgG2b, and IgG3 subclasses [24].
• Cloning of dnaK and dnaJ homologous genes from a purple non-sulfur bacterium Rhodopseudomonas species [25].
• The dnaK and dnaJ genes were isolated as a cluster from a purple non-sulfur phototrophic bacterium, Rhodopseudomonas species No. 7 by a polymerase chain reaction (PCR) based method [25].
• However, as in the related organism Rhodopseudomonas blastica, neither genes for components of F0, the membrane sector of ATP synthase, nor a homologue of the E. coli uncI gene are associated with this locus, as they are in E. coli [26].
• Laser-spectroscopic data obtained with non-crystallized, isolated LH2 of Rhodospirillum molischianum are in line with a highly symmetric (C8) circular aggregate, but deviations have been found for LH2 of Rhodobacter sphaeroides and Rhodopseudomonas acidophila [27].

Analytical, diagnostic and therapeutic context of Rhodopseudomonas

• Proton nuclear magnetic resonance studies of the ligation states of the monomeric ferricytochrome c' from Rhodopseudomonas palustris. Modulation of axial histidine bonding via variable proton donation [28].
• Sodium alkyl ether sulfate (AES), an analog of sodium dodecyl sulfate (SDS) was used in polyacrylamide gel electrophoresis (PAGE) for the partial decomposition of the photosynthetic reaction center (RC) of Rhodopseudomonas viridis [29].
• Light and heavy membrane fractions have been isolated by equilibrium sucrose density centrifugation from Rhodopseudomonas capsulata 938 GCM grown aerobically in the dark (chemotrophically) and anaerobically in the light (phototrophically) [30].
• Crystallization and subunit composition of citrate lyase of Rhodopseudomonas gelatinosa [31].
• The enzyme was purified of fructose bisphosphatase activity from Rhodopseudomonas capsulata by means of affinity chromatography and was shown to have a native molecular weight of about 220,000 [32].

References