Possible initial events of photophosphorylation in membranes of Rhodopseudomonas viridis and Rhodopseudomonas capsulata Ala+r.
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Adenosine Diphosphate↗
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Cytochrome c2--reaction centre coupling in chromatophores of Rhodopseudomonas sphaeroides and Rhodopseudomonas capsulata.
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Antimycin A↗
Localization of the reaction-centre subunits in the intracytoplasmic membranes of Rhodopseudomonas sphaeroides and Rhodopseudomonas capsulata [proceedings].
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Bacterial Chromatophores↗
Comparison of phototrap complexes from chromatophores of Rhodospirillum rubrum, Rhodopseudomonas spheroides, and the R-26 mutant of Rhodopseudomonas spheroides.
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Bacterial Chromatophores↗
Transfer of Rhodopseudomonas acidophila to the new genus Rhodoblastus as Rhodoblastus acidophilus gen. nov., comb. nov.
Rhodopseudomonas acidophila has unique properties among the phototrophic alpha-Proteobacteria and is quite distinct from the type species of Rhodopseudomonas, Rhodopseudomonas palustris. Therefore, the transfer of Rhodopseudomonas acidophila to Rhodoblastus acidophilus gen. nov., comb. nov., is proposed. This proposal is in accordance with other taxonomic reclassifications proposed previously and fully reflects the phylogenetic distance from Rhodopseudomonas palustris.
DNA, Ribosomal↗
Development of a gene cloning system for the hydrogen-producing marine photosynthetic bacterium Rhodopseudomonas sp.
Seventy-six strains of marine photosynthetic bacteria were analyzed by agarose gel electrophoresis for plasmid DNA content. Among these strains, 12 carried two to four different plasmids with sizes ranging from 3.1 to 11.0 megadaltons. The marine photosynthetic bacterium Rhodopseudomonas sp. NKPB002106 had two plasmids, pRD06S and pRD06L. The smaller plasmid, pRD06S, had a molecular weight of 3.8 megadaltons and was cut at a single site by restriction endonucleases SalI, SmaI, PstI, XhoI, and BglII. Moreover, the marine photosynthetic bacterium Rhodopseudomonas sp. NKPB002106 containing plasmid pRD06 had a satisfactory growth rate (doubling time, 7.5 h), a hydrogen-producing rate of 0.96 mumol/mg (dry weight) of cells per h, and nitrogen fixation capability. Plasmid pRD06S, however, had neither drug resistance nor heavy-metal resistance, and its copy number was less than 10. Therefore, a recombinant plasmid consisting of pRD06S and Escherichia coli cloning vector pUC13 was constructed and cloned in E. coli. The recombinant plasmid was transformed into Rhodopseudomonas sp. NKPB002106. As a result, Rhodopseudomonas sp. NKPB002106 developed ampicillin resistance. Thus, a shuttle vector for gene transfer was constructed for marine photosynthetic bacteria.
Ampicillin↗
Isolation and characterization of a temperate bacteriophage specific for Rhodopseudomonas spheroides.
The isolation of a temperature phage specific for the photosynthetic bacterium Rhodopseudomonas spheroides is reported. This phage, Rphi-1, establishes a state of lysogeny and can be induced from the prophage state by exposure to mitomycin C or UV irradiation. Mutants of Rphi-1 which grow on a standard laboratory strain (2.4.1) of Rhodopseudomonas spheroides were isolated. Although the original Rphi-1 isolated was chloroform sensitive, the mutant which plates on strain 2.4.1 is chloroform resistant. Rphi-1 does not grow on closely related bacteria, such as Rhodopseudomonas palustris or Rhodopseudomonas capsulata. Rphi-1 mutants forms plaques with the same efficiency whether the plates are incubated under aerobic conditions in the dark or under anaerobic conditions in the light (phototropic conditions).
Anaerobiosis↗
Structural aspects of the dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila.
1. A dye-linked alcohol dehydrogenase was purified 60-fold from extracts of Rhodopseudomonas acidophila 10050 grown aerobically on ethanol. 2. The properties of this enzyme were identical with those of the alcohol dehydrogenase synthesized by this organism during growth on methanol anaerobically in the light, and they are judged to be the same enzyme. 3. The enzyme gave a single protein band, coincident with alcohol dehydrogenase activity, during electrophoresis on polyacrylamide gel. 4. The amino acid composition, ioselectric point, u.v. and visible absorption spectra of the enzyme were determined and compared with those of other similar enzymes. 5. The presence of 0.7--1.0 g-atom of non-haem, acidlabile iron/mol of enzyme was shown by atomic absorption spectrophotometry and colorimetric assay. The iron could not be dissociated from the enzyme by dialysis against chelating agents. 6. E.p.r. spectroscopy of the enzyme did not indicate any redox function for the iron during alcohol dehydrogenation, but showed a signal at g = 2.00 consistent with the presence of a protein-bound organic free radical. 8. Antisera were raised against alcohol (methanol) dehydrogenases purified from Rhodopseudomonas acidophila, Paracoccus denitrificans and Methylophilus methylotrophus. 9. The antiserum to the Rhodopseudomonas acidophila enzyme cross-reacted with neither of the two other antisera, nor with crude extracts of methanol-grown Hyphomicrobium X and Pseudomonas AM1, thus emphasizing its singular biochemical properties.
Alcohol Oxidoreductases↗
Comparative studies of protein properties and bacteriochlorophyll contents of bacteriochlorophyll-protein complexes from spectrally different types of Rhodopseudomonas palustris.
The amino acid compositions, constituent polypeptides and bacteriochlorophyll (Bchl) contents of two kinds of Bchl-protein complexes isolated from Rhodopseudomonas palustris were examined. Spectrally dissimilar intracytoplasmic membranes obtained from cells cultured under different conditions were used as starting materials. The B870-reaction center complex was consistent in its amino acid composition, constituent polypeptides and Bchl content, as well as in its near-infrared absorption spectrum. B800-850 complexes from the different types of intracytoplasmic membrane varied in their absorption spectra, though they had similar amino acid compositions and were comprised of basically similar kinds of polypeptides with variations only in the levels of some minor constituent polypeptides. The B800-850 complex with a low absorption peak at 850 nm had a Bchl content 1.3 times greater than the B800-850 complex with a high absorption peak at 850 nm. These results indicate that the B800-850 complex from R. palustris contains more components (both polypeptides and Bchl molecules) than the B800-850 complexes from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides.
Amino Acids↗
Rhodopseudomonas rhenobacensis sp. nov., a new nitrate-reducing purple non-sulfur bacterium.
During the course of isolating and identifying purple non-sulfur bacteria, one nitrate-reducing strain was isolated which did not fit the description of any other purple non-sulfur bacterium known to date. The isolate had rod-shaped cells that contained lamellar intracytoplasmic membranes and produced red cultures. Absorption maxima of photosynthetically grown cell homogenates were at 376, 471, 503, 540, 591, 805 and 878 nm. The new isolate grew anaerobically in the light or aerobically in the dark. Various organic compounds served as carbon sources and electron donors. The predominant quinone was ubiquinone 10, the predominant fatty acid was 18:1omega7c. The polar lipids comprised diphosphatidyl glycerol, phosphatidyl glycerol, phosphatidyl ethanolamine and phosphatidyl choline. Analysis of the 16S rDNA gene sequences revealed that the new isolate was closely related to Rhodopseudomonas palustris. A DNA-DNA- hybridization study differentiated the new isolate and Rhodopseudomonas palustris at the species level. Therefore, the name Rhodopseudomonas rhenobacensis sp. nov. is proposed for the new isolate.
Aerobiosis↗
Rhodopseudomonas faecalis sp. nov., a phototrophic bacterium isolated from an anaerobic reactor that digests chicken faeces.
Five isolates of a previously undescribed species of purple non-sulfur phototrophic bacteria were characterized. They were Gram-negative, had mobile, budding vibrioid cells and contained lamellar intracytoplasmic membranes. Cultures produced red pigments in the light. Live cells of photosynthetic cultures exhibited absorption maxima at 382, 460-464, 494-496, 534-538, 596, 804-806 and 870-874 nm, indicating the presence of bacteriochlorophyll a and carotenoids belonging to the spirilloxanthin series in cells. The new isolates grew anaerobically or microaerobically in the light, but not aerobically in the dark. Optimal growth occurred at 35-40 degrees C and at pH 6.5-8.5. Various organic compounds were used as photosynthetic electron donors and carbon sources. Sulfate was used as sulfur source for growth. Ubiquinone 10 was synthesized as the major quinone. A phylogenetic analysis based on 16S rRNA gene sequences revealed that strain gc(T), a representative of the new isolates, was closest to Rhodopseudomonas palustris, with a similarity of 97.5%. DNA-DNA hybridization further distinguished strain gc(T) from Rhodopseudomonas palustris at the species level. Therefore, the name Rhodopseudomonas faecalis sp. nov. was proposed for the new isolates. The type strain is gc(T) ( = AS1.2176(T) = JCM 11668(T)).
Animals↗
Succinate dehydrogenase in Rhodopseudomonas sphaeroides: subunit composition and immunocross-reactivity with other related bacteria.
Antibodies were raised against the succinate dehydrogenase (SDH) present in the chromatophores of phototrophically grown Rhodopseudomonas sphaeroides. Crossed immunoelectrophoresis experiments indicated that the SDH present in the cytoplasmic membranes of heterotrophically grown R. sphaeroides is probably the same enzyme observed in the chromatophores. The enzyme was extracted by Triton X-100 in a form which consisted of only two subunits (molecular weight, 68,000 and 30,000) and was not associated with a cytochrome b. The antibodies directed against SDH from R. sphaeroides showed no immunocross-reactivity with SDH from phylogenetically related bacterial species, including Rhodopseudomonas capsulata, Paracoccus denitrificans, Rhodopseudomonas palustris, Rhodospirillum rubrum, and Rhodospirillum fulvum.
Bacterial Chromatophores↗
Nitrous oxide reduction by members of the family Rhodospirillaceae and the nitrous oxide reductase of Rhodopseudomonas capsulata.
After growth in the absence of nitrogenous oxides under anaerobic phototrophic conditions, several strains of Rhodopseudomonas capsulata were shown to possess a nitrous oxide reductase activity. The enzyme responsible for this activity had a periplasmic location and resembled a nitrous oxide reductase purified from Pseudomonas perfectomarinus. Electron flow to nitrous oxide reductase was coupled to generation of a membrane potential and inhibited by rotenone but not antimycin. It is suggested that electron flow to nitrous oxide reductase branches at the level of ubiquinone from the previously characterized electron transfer components of R. capsulata. This pathway of electron transport could include cytochrome c', a component hitherto without a recognized function. R. capsulata grew under dark anaerobic conditions in the presence of malate as carbon source and nitrous oxide as electron acceptor. This confirms that nitrous oxide respiration is linked to ATP synthesis. Phototrophically and anaerobically grown cultures of nondenitrifying strains of Rhodopseudomonas sphaeroides, Rhodopseudomonas palustris, and Rhodospirillum rubrum also possessed nitrous oxide reductase activity.
Acetylene↗
[Bacteriochlorophyll a synthesis in Rhodopseudomonas palustris].
By means of electron microscope it was demonstrated that photosynthetically-grown Rhodopseudomonas palustris exhibits an intracytoplasmic membrane system (Figure 1a), which is not observed in aerobically-dark grown bacteria (Figure 1b). The content of bacteriochlorophyll alpha and the enzyme activity of succinil-CoA-synthetase, ALA-sinthetase and ALA-dehydratase in several media grown Rhodopseudomonas palustris could be measured. Aerobically-dark grown cells do not synthetize bacteriochlorophyll alpha and the activity of ALA-synthetase is lower than in photosynthetically-grown cells (Table 1), suggesting a possible regulatory role for this enzyme in the pigment biosynthesis. Some inhibitors of electron transport and uncouplers of photophosphorylation inhibit both the bacterial growth and bacteriochlorophyll alpha biosynthesis (Table 2), while the levels of ALA-synthetase are not affected. If the incubation in the presence of these kinds of compounds is prolongated, the effects disappear. Although the regulatory role of ALA-synthetase should be very important, apparently it would not be the unique regulatory factor for bacteriochlorophyll alpha biosynthesis in Rhodopseudomonas palustris.
5-Aminolevulinate Synthetase↗
Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation.
Protein electrochemistry in an ultra-thin-layer electrochemical cell suitable for UV/vis and IR spectroscopy has been used to characterize the vibrational modes of the primary electron donors of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers in their neutral and cation radical states (P and P+, respectively). The P-->P+ redox transitions could be well separated from redox reactions of other cofactors according to their redox midpoint potential. The IR difference bands of the primary electron donor bacteriochlorophylls all titrate in unison and exhibit the correct midpoint potential. Comparison of the difference spectra with those of isolated bacteriochlorophylls a and b in organic solvents of different polarity and proton activity [Mäntele, W., Wollenweber, A. M., Nabedryk, E., & Breton, J. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 8468-8472] leads to similar conclusions on the binding and interaction of the pigments within the protein matrix as previously obtained from light-induced P+Q-/PQ difference spectra. Equilibration of the reaction centers in D2O leads to few but distinct shifts of bands and changes of band intensities at 1662, 1634, and 1526 cm-1 (Rhodobacter sphaeroides) and 1694, 1664, 1648, 1630, and 1532 cm-1 (Rhodopseudomonas viridis) as well as to smaller deviations at other wavenumbers. The H-->D-sensitive band at 1662 cm-1 is interpreted in terms of a histidine NH2+ bending mode. A second H/D-sensitive difference band around 1648 cm-1 in the Rhodopseudomonas viridis reaction center may be associated with the peptide C = O of one of the amino acids surrounding P [eventually of the histidine(s) ligating the Mg] which is affected by P+ formation.(ABSTRACT TRUNCATED AT 250 WORDS)
Cations↗
[Variants of the plasmid pAS8 delta with increased frequency of integration into Rhodopseudomonas sphaeroides chromosome--the result of IS8-element duplication].
The possible participation of IS8 and IS elements of Rhodopseudomonas sphaeroides in cointegrate formation by chromosome of the purple bacterium and plasmid pAS8-121 delta has been studied. The plasmid derivatives having deleted Tn7 have been studied. Plasmid integration into the chromosome of the purple bacterium is shown to be mediated by IS8 element of the plasmid. Plasmid derivatives having the integration potential increased for two orders were isolated by a series of intergeneric conjugational crosses during which plasmid pAS8-121 delta was transferred from Rhodopseudomonas sphaeroides (cointegrate of plasmid and chromosome) to Escherichia coli (plasmid in an autonomous state) and back to Rhodopseudomonas sphaeroides. The restriction analysis of plasmid DNA digested by Hpal and Smal restriction endonucleases has revealed the tandem duplications of IS8 in plasmids capable of integration into the chromosome of the purple bacterium with a high frequency.
Chromosomes, Bacterial↗
COFACTOR-DEPENDENT ALDOSE DEHYDROGENASE OF RHODOPSEUDOMONAS SPHEROIDES.
Niederpruem, Donald J. (University of California, Berkeley), and Michael Doudoroff. Cofactor-dependent aldose dehydrogenase of Rhodopseudomonas spheroides. J. Bacteriol. 89:697-705. 1965.-Particulate enzyme preparations of cell extracts of Rhodopseudomonas spheroides possess constitutive dehydrogenase and oxidase activities for aldose sugars, reduced nicotinamide adenine dinucleotide (NADH(2)), and succinate. The dehydrogenation of aldoses requires an unidentified cofactor which is not required for the oxidation of succinate nor of NADH(2). The cofactor is present in the particulate fraction of aerobic cells, but is unavailable to the enzyme system. It can be liberated by boiling or by treatment with salts at high concentration. The cofactor also appears in the soluble fraction of aerobic cells, but only after exponential growth has ceased. Extracts of cells grown anaerobically in the light possess the apoenzyme, but not the cofactor, for aldose oxidation. Cofactor activity was found in extracts of Bacterium anitratum (= Moraxella sp.) but not in Escherichia coli, Pseudomonas fluorescens, yeast, or mouse liver. In 0.075 m tris(hydroxymethyl)aminomethane-phosphoric acid buffer (pH 7.3), the oxidation of NADH(2) was stimulated and succinoxidase was inhibited by high salt concentrations.
Alcohol Oxidoreductases↗
L-methionine-SR-sulfoximine as a probe for the role of glutamine synthetase in nitrogenase switch-off by ammonia and glutamine in Rhodopseudomonas palustris.
Methionine sulfoximine (MSX), an irreversible inhibitor of glutamine synthetase of Rhodopseudomonas palustris restored nitrogenase activity to cells in which nitrogenase had been completely inhibited by ammonia switch-off. After addition of MSX, there was a lag period before nitrogenase activity was fully restored. During this lag, glutamine synthetase activity progressively decreased, and near the time of its complete inhibition, nitrogenase activity resumed. Nitrogenase switch-off by ammonia thus required active glutamine synthetase. Glutamine itself caused nitrogenase inhibition whose reversal by MSX depended on the relative ratio of MSX to glutamine. Unlike ammonia, glutamine inhibited nitrogenase under conditions where glutamine synthetase activity was absent. This indicates that glutamine is the effector molecule in nitrogenase switch-off, for instance by interacting with the enzymatic system for Fe protein inactivation. The effects of glutamine and MSX were also dependent on the culture age. Possible explanation for this and for the competitive effects are a common binding site within the regulatory apparatus for nitrogenase, or, in part, within a common transport system. Some observations with MSX were extended to Rhodopseudomonas capsulata and agreed with those in R. palustris.
Ammonia↗