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At least 19 recordsLinked to original sources
PubMed1998

Reclassification of species of the spiral-shaped phototrophic purple non-sulfur bacteria of the alpha-Proteobacteria: description of the new genera Phaeospirillum gen. nov., Rhodovibrio gen. nov., Rhodothalassium gen. nov. and Roseospira gen. nov. as well as transfer of Rhodospirillum fulvum to Phaeospirillum fulvum comb. nov., of Rhodospirillum molischianum to Phaeospirillum molischianum comb. nov., of Rhodospirillum salinarum to Rhodovibrio salexigens.

The 165 rDNA sequence of Rhodospirillum mediosalinum was determined and compared with corresponding sequences from other spiral-shaped purple non-sulfur bacteria classified as or related to the genus Rhodospirillum in the alpha subclass of the Proteobacteria. Sequence similarities separate the currently recognized Rhodospirillum species into five different groups with no more than 91% sequence similarity, clearly indicating the necessity to recognize these groups as different genera. Major diagnostic properties of these bacteria are compared and new genera Phaeospirillum gen. nov., Roseospira gen. nov., Rhodothalassium gen. nov. and Rhodovibrio gen. nov. are described with the species Phaeospirillum fulvum comb. nov., Phaeospirillum molischianum comb. nov., Rhodovibrio salinarum comb. nov., Rhodovibrio sodomensis comb. nov., Rhodothalassium salexigens comb. nov. and Roseospira mediosalina comb. nov. The genus Rhodospirillum is represented by Rhodospirillum rubrum and Rhodospirillum photometricum and an emended description of this genus is also given.

Base Composition↗
PubMed1989

Extended X-ray absorption fine structure study of Rhodospirillum rubrum and Rhodospirillum molischianum cytochromes c': relationship between heme stereochemistry and spin state.

An EXAFS study on the oxidized and reduced forms of cytochromes c' from Rhodospirillum rubrum and Rhodospirillum molischianum was performed at pH 7. The cytochromes c' have an apparent coordination number of 5 in both oxidation states. Average Fe-ligand bond lengths of 2.02 +/- 0.025 and 2.06 +/- 0.025 A are obtained in their oxidized and reduced forms, respectively. By use of suitable values for the Fe-NHis bond length and Fe out-of-plane displacement, as determined by small molecule crystallographic techniques, the Fe-Npyrrole bond lengths and the porphyrin center-to-Npyrrole distance have been estimated for cytochrome c' in both of its oxidation states. With this model, estimates of the Fe-Npyrrole bond lengths are 2.01 +/- 0.03 and 2.05 +/- 0.03 A, for the oxidized and reduced cytochromes c', respectively. The center-to-Npyrrole distance is estimated to be 1.99 +/- 0.03 A for oxidized cytochrome c' and 2.03 +/- 0.03 A for reduced cytochrome c'.

Cytochrome c Group↗
PubMed1996

Comparison of the structural requirements for bacteriochlorophyll binding in the core light-harvesting complexes of Rhodospirillum rubrum and Rhodospirillum sphaeroides using reconstitution methodology with bacteriochlorophyll analogs.

Bacteriochlorophyll (BChl) structural requirements for formation of the core light-harvesting complex (LH1) and its structural subunit complex were examined by reconstitution with BChl analogs and the alpha- and beta-polypeptides of Rhodospirillum rubrum and Rhodobacter sphaeroides. Comparable results were obtained with most of the BChl analogs and the polypeptides of each bacterium, indicating the conservation of BChl binding sites. These systems showed the following common requirements for formation of the subunit complex and LH1: (1) Mg or a metal of similar size and coordination chemistry (e.g., Zn, Cd, Ni), (2) a bacteriochlorin oxidation state of the macrocyclic ring, (3) a 13(2)-carbomethoxy group, and (4) an intact ring V. Some structural features were not as critically important. For example, the subunit complex and LH1 could be formed with both sets of polypeptides and BChl b, as well as with analogs containing either short (ethanol) or long (phytol) esterifying alcohols. Two derivatives were identified that behave differently with the two sets of polypeptides. The 3-acetyl group is required to form LH1 in both bacteria, although a subunit-type complex was readily formed with [3-vinyl]BChl a and the polypeptides of Rs. rubrum but formed only slightly under special conditions with polypeptides of Rb. sphaeroides. [13(2)-OH]BChl a(p) formed both subunit- and LH1-type complexes with the alpha- and beta-polypeptides of Rb. sphaeroides but not with those of Rs. rubrum. Thus, some subtle differences in the BChl binding sites exist in the LH1 complexes of these two bacteria.

Amino Acid Sequence↗
PubMed1984

The light-harvesting polypeptides of Rhodospirillum rubrum. I. The amino-acid sequence of the second light-harvestng polypeptide B 880-beta (B 870-beta) of Rhodospirillum rubrum S 1 and the carotenoidless mutant G-9+. carotenoidless mutant G-9+.

The light-harvesting complex B 880 from Rhodospirillum rubrum S 1 (wild type) and B 870 from the carotenoidless mutant G-9+ was shown to consist mainly of an organic solvent-(chloroform/methanol-) soluble and an organic solvent-insoluble polypeptide. The isolation and separation of these two low-molecular-mass polypeptides (Mr 6101 and Mr 6079) were achieved by a two-step extraction procedure of chromatophores using in the first step chloroform/methanol containing 0.1M ammonium acetate. Following Sephadex LH-60 chromatography of this first extract a light-harvesting polypeptide (B 870-alpha) was isolated and its complete amino acid sequence was determined (R. Brunisholz et al. (1981) FEBS Lett. 129/1, 150-154, B 880-alpha: G. Gogel et al. (1983) Biochim. Biophys. Acta 746, 32-39). Upon reextraction of the chromatophore pellet with chloroform/methanol/ammonium acetate containing in addition acetic acid a second low-molecular-mass polypeptide (B 880-beta of B 870-beta) was generated. The complete amino acid sequences of the chloroform/methanol-insoluble light-harvesting polypeptide of Rs. rubrum S 1 (B 880-beta) and of Rs. rubrum G-9+ (B 870-beta) were determined. They are identical and consist of 54 amino acid residues. The conserved histidine residue within the hydrophobic stretch raises more evidence for ligand complexation of bacteriochlorophyll to this specific histidine residue which therefore possibly plays the key role in pigment-protein interactions. Both polypeptides (B 880-alpha and B 880-beta) are part of the light-harvesting complex B 880 in an apparent ratio of 1:1. Based on the primary structure data a possible arrangement of both light-harvesting polypeptides within the membrane will be discussed.

Amino Acid Sequence↗
PubMed1987

The reaction domain on Rhodospirillum rubrum cytochrome c2 and horse cytochrome c for the Rhodospirillum rubrum cytochrome bc1 complex.

The interaction of the Rhodospirillum rubrum cytochrome bc1 complex with R. rubrum cytochrome c2 and horse cytochrome c was studied using specific lysine modification and ionic strength dependence methods. In order to define the reaction domain on cytochrome c2, several fractions consisting of mixtures of singly labeled carboxydintrophenyl-cytochrome c2 derivatives were employed. Fraction A consisted of a mixture of derivatives modified at lysines 58, 81, and 109 on the back of cytochrome c2, while fractions C1, C2, C3, and C4 were mixtures of singly labeled derivatives modified at lysines 9, 13, 75, 86, and 88 on the front of cytochrome c2 surrounding the heme crevice. The rate of the reaction of fraction A was found to be nearly the same as that of native cytochrome c2. However, the rate constants of fractions C1-C4 were found to be more than 20-fold smaller than that of native cytochrome c2. These results indicate that lysine residues surrounding the heme crevice of cytochrome c2 are involved in electrostatic interactions with carboxylate groups at the binding site on the cytochrome bc1 complex. Since the same domain is involved in the reaction with the photosynthetic reaction center, cytochrome c2 must undergo some type of rotational or translational diffusion during electron transport in R. rubrum. The reaction rates of horse heart cytochrome c derivatives modified at single lysine amino groups with trifluoroacetyl or trifluoromethylphenylcarbamoyl were also measured. Modification of lysines 8, 13, 25, 27, 72, 79, and 87 surrounding the heme crevice was found to significantly lower the rate of the reaction, while modification of lysines in other regions had no effect. This indicates that the reaction of horse cytochrome c also involves the heme crevice domain.

Animals↗
PubMed1984

The light-harvesting polypeptides of Rhodospirillum rubrum. II. Localisation of the amino-terminal regions of the light-harvesting polypeptides B 870-alpha and B 870-beta and the reaction-centre subunit L at the cytoplasmic side of the photosynthetic membrane of Rhodospirillum rubrum G-9+.

The unspecific proteinase K and the specific proteases alpha-chymotrypsin, trypsin and S. aureus V 8 protease were used in order to determine the orientation of the polypeptides B 870-alpha and B 870-beta from the major antenna complex B 870 of Rs. rubrum G-9+ within the chromatophore membrane (inside-out vesicle). Although B 870-alpha exhibits cleavable peptide bonds, treatment with specific proteases yielded splitting only in B 870-beta within the N-terminal region. In the case of proteinase K, which was most effective, mainly 6 (B 870-alpha) and 16 (B 870-beta) amino acid residues were removed from their N-terminal parts as proved by means of Edman degradation of cleavage products. The major peptide bonds cleaved were identified as Gln6-Leu7 in B 870-alpha and as Lys16-Glu17 in B 870-beta. The central hydrophobic stretch regions and the relatively hydrophilic C-terminal parts of both light-harvesting polypeptides were not affected by proteinase K. On the basis of these degradation experiments a transmembrane orientation of B 870-alpha and B 870-beta is postulated, with their N-terminal towards the cytoplasm and their C-termini towards periplasm with regard to the photosynthetic membrane. This hypothesis is supported by the transmembrane model proposed by Brunisholz et al. (Hoppe-Seyler's Z., Physiol. Chem., (1984) 365, 675-688) in which the hydrophobic stretch of B 870-alpha and of B 870-beta forming an alpha-helix would span the membrane once. Organic solvent extraction of chromatophores treated with proteinase K yielded a fairly pure polypeptide fragment with an apparent molecular mass of 14000 Da. Its N-terminal amino-acid sequence is identical with the sequence within the N-terminal region of the reaction centre subunit L of Rs. rubrum G-9+. Thus it is most likely that as in the case of B 870-beta, proteinase K removed 16 amino acid residues from the N-terminal part of subunit L. This subunit therefore also seems to be exposed at the surface of the cytoplasmic side of the chromatophore membrane.

Amino Acids↗
PubMed2002

Rhodospirillum rubrum possesses a variant of the bchP gene, encoding geranylgeranyl-bacteriopheophytin reductase.

The bchP gene product of Rhodobacter sphaeroides is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol; here, we show that this enzyme also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin (Bphe). In contrast, we demonstrate that a newly identified homolog of this gene in Rhodospirillum rubrum encodes an enzyme, GG-Bphe reductase, capable of reducing the isoprenoid moiety of Bphe only. We propose that Rhodospirillum rubrum is a naturally occurring bchP mutant and that an insertion mutation may have been the initial cause of a partial loss of function. Normal BchP function can be restored to Rhodospirillum rubrum, creating a new transconjugant strain possessing Bchl esterified with phytol. We speculate on the requirement of Rhodospirillum rubrum for phytylated Bphe and on a potential link between the absence of LH2 and of phytylated Bchl from the wild-type bacterium. The identification of a second role for the fully functional BchP in catalyzing the synthesis of phytylated Bphe strongly suggests that homologs of this enzyme may be similarly responsible for the synthesis of phytylated pheophytin in organisms possessing photosystem 2. In addition to bchP, other members of a photosynthesis gene cluster were identified in Rhodospirillum rubrum, including a bchG gene, demonstrated to encode a functional Bchl synthetase by complementation of a Rhodobacter sphaeroides mutant.

Amino Acid Sequence↗
PubMed1981

Biosynthesis of bacterial glycogen: activator specificity of the adenosine diphosphate glucose pyrophosphorylases from the genus Rhodospirillum.

The adenosine diphosphate (ADP) glucose pyrophosphorylases from Rhodospirillum fulvum, Rhodospirillum molischianum, and Rhodospirillum tenue were partially purified, and their kinetic properties were studied. The enzyme from the three organisms was found to be activated by pyruvate and thus was similar to the Rhodospirillum rubrum enzyme that had been previously studied (C. E. Furlong, and J. Preiss, J. Biol. Chem. 244:2539-2548, 1979). The enzymes from R. fulvum, R. molischianum, and R. tenue were also activated by oxamate, an analog of pyruvate. Other alpha-keto acids, alpha-ketobutyrate and hydroxypyruvate, activated to a smaller extent. The presence of pyruvate increased the apparent affinity for adenosine 5'-triphosphate and MgCl2 for all three enzymes. The R. molischianum enzyme has very little sensitivity to inhibition by adenosine 5'-monophosphate, ADP, or inorganic phosphate. However, R. tenue ADPglucose pyrophosphorylase is very sensitive to inhibition by adenosine 5'-monophosphate, and the R. fulvum enzyme is inhibited by ADP. Increasing pyruvate concentration reversed the inhibition caused by adenosine 5'-monophosphate or ADP. Since ADPglucose is the glycosyl donor for synthesis of glycogen, it is possible that in vivo glycogen synthesis is regulated by the concentration of pyruvate and, in the case of R. fulvum and R. tenue, by the ratio of pyruvate concentration to inhibitor concentration.

Adenosine Diphosphate Glucose↗
PubMedDate not supplied

The puh structural gene coding for the H subunit of the Rhodospirillum rubrum photoreaction center.

The Rhodospirillum rubrum structural gene puh, coding for the photoreaction center H polypeptide, and three other putative genes that surround puh were cloned and sequenced. The deduced 257 amino acid H polypeptide has a molecular weight of 27,909, in close agreement with polyacrylamide gel electrophoresis determination. Hydropathy plots predict a single hydrophobic alpha helix. The H polypeptide of Rhodospirillum rubrum shares only 23% of its residues with all three of the H polypeptides from Rhodopseudomonas viridis, Rhodobacter capsulatus, and Rhodobacter sphaeroides. Despite this apparent low degree of similarity, statistical analysis leaves no doubt about their close relatedness. Interspecies evolutionary distance, assessed by this analysis, confirms the closeness of the two Rhodobacter species, Rhodospirillum rubrum and Rhodopseudomonas viridis being approximately equidistant from them. Three regions of the H polypeptide are highly conserved in all four species. They correspond to known contact points of H with the complex of the other two (L and M) subunits on the cytoplasmic side of the membrane. A glutamic acid residue (H polypeptide residue 177), conserved in the other bacteria and suggested to be involved in the binding of secondary quinone QB, is replaced by serine in Rhodospirillum rubrum. The open reading frames G115, I2372, and I3087 are predicted to, respectively, encode polypeptides of 480, 224, and 155 residues coiled in 10, 2, and 1 transmembrane helices. Open reading frame G115 shares 56% identical residues with F1696, a sequence arranged in the genome of Rhodobacter capsulatus. The gene product of ORF I3087 is predicted to share highly similar sequences with nitrogenase reductase (encoded by nifH) of 11 different bacterial species and is suggested to have a regulatory function.

Amino Acid Sequence↗
PubMed1976

A possible physiological function of the oxygen-photoreducing system of Rhodospirillum rubrum.

Anaerobic suspensions of Rhodospirillum rubrum cells which had been grown in the dark under low oxygen tension showed only a small increase of their ATP content when illuminated for 30 s. The same suspensions failed to start immediate growth in the light. Both high light-induced ATP levels and immediate phototrophic growth were elicited by small amounts of oxygen which were insufficient by themselves to raise the ATP levels or to support growth in the dark. The oxygen requirement for growth disappeared after some time of anaerobic illumination and was not observed in suspensions of cells which had been grown in the light under anaerobiosis. Furthermore, these phototrophic cells reached the maximum levels of ATP when illuminated in the absence of oxygen. Strain F11, a mutant derivative of Rhodospirillum rubrum which lacked the ability to photoreduce oxygen in vitro, needed abnormally high amounts of oxygen to increase its ATP levels and to grow in the light. Besides, KCN inhibited the increase of ATP levels in illuminated mutant cells but not in wild type cells. An additional difference between both strains was that the oxygen requirement for growth did not disappear in the mutant after some time of anaerobic incubation in the light. To explain these observations, it is proposed that the photosynthetic system of semiaerobically-grown Rhodospirillum rubrum becomes overreduced under anaerobiosis. The oxygen-photoreducing system, which is impaired in the mutant is apparently used to oxidize the photosynthetic system to its optimal redox state, carrying electrons to oxygen or to other endogenous acceptors which are formed during incubation in the light. The mutant seems to replace the defective system by a cyanide-sensitive pathway which may reduce oxygen but not the alternative endogenous acceptors.

Adenosine Triphosphate↗
PubMed1998

The respiratory chain of the halophilic anoxygenic purple bacterium Rhodospirillum sodomense.

The halophilic purple nonsulfur bacterium Rhodospirillum sodomense has been previously described as an obligate phototroph that requires yeast extract and a limited number of organic compounds for photoheterotrophic growth. In this work, we report on chemoheterotrophic growth of R. sodomense in media containing either acetate or succinate supplemented with 0.3-0.5% yeast extract. Plasma membranes isolated from cells grown aerobically in the dark contained three b-type and three c-type membrane-bound cytochromes with Em,7 of +171 +/- 10, +62 +/- 10 and -45 +/- 13 mV (561-575 nm), and +268 +/- 6, +137 +/- 10 and -43 +/- 12 mV (551-540 nm). A small amount of a soluble c-type cytochrome with a mol. mass of 15 kDa (Em, 7 >/= +150 mV) was identified. Spectroscopic and immunological methods excluded the presence of cytochrome of the c2 class and high-potential iron-sulfur proteins. Inhibitory studies indicated that only 60-70% of the respiratory activity was blocked by low concentrations of cyanide, antimycin A, and myxothiazol (10, 0.1, and 0.2 microM, respectively). These results were interpreted to show that the oxidative electron transport chain of R. sodomense is branched, leads to a quinol oxidase that is fully blocked by 1 mM cyanide and that is involved in light-dependent oxygen reduction, and leads to a cytochrome c oxidase that is inhibited by 10 microM cyanide. These features taken together suggest that R. sodomense differs from the closely related species Rhodospirillum salinarum and from other species of the genus Rhodospirillum in that it contains multiple membrane-bound cytochromes c.

Acetates↗
PubMed1985

Structure of ferricytochrome c' from Rhodospirillum rubrum at 6 A resolution.

The structure of a ferricytochrome c' extracted from Rhodospirillum rubrum has been determined at 6 A resolution by the X-ray crystallographic method. The crystals, obtained by dialyzing the protein solution against polyethylene glycol 4000, belong to the hexagonal space group P6(1). Two heavy atom derivatives were obtained by soaking the native crystals in K2PtCl6 and CH3HgCl solution. The phases calculated by the multiple isomorphous replacement method gave an overall figure of merit of 0.90 at 6 A resolution. The resulting electron density map showed the molecular boundary clearly, and gave molecular dimensions of 50 X 25 X 30 A for a monomer molecule. From visual examination of this map, the cytochrome c' from Rhodospirillum rubrum has a similar chain-folding pattern to the cytochrome c' from Rhodospirillum molischianum, the structure determination of which has already been carried out.

Crystallography↗
PubMed1962

Metabolism of sulfate by the chromatophore of Rhodospirillum.

Ibanez, M. L. (The Pennsylvania State University, University Park) and E. S. Lindstrom. Metabolism of sulfate by the chromatophore of Rhodospirillum. J. Bacteriol. 84:451-455. 1962.-The chromatophore of Rhodospirillum rubrum was shown to possess enzymes for the activation and reduction of inorganic sulfate. The chromatophore was able to synthesize 3'-phosphoadenosine 5'-phosphosulfate (PAPS), using either exogenous adenosine triphosphate (ATP) or ATP synthesized via photophosphorylation. Light was required for the reduction of sulfate to a volatile form, presumably sulfite. Light enhanced the incorporation of sulfate-sulfur into cystine, cysteine, and cysteic acid of the chromatophore. This incorporation was probably the result of exchange reactions of reduced sulfur, not the result of net synthesis. The 100:1 ratio of the activation to reduction of sulfate and the inhibition of the reduction by exogenous ATP suggested that PAPS might not be the substrate for chromatophoral sulfate reduction.

Adenine Nucleotides↗
PubMed1965

LOCATION OF CHLOROPHYLL IN RHODOSPIRILLUM RUBRUM.

Holt, Stanley C. (University of California, Davis), and Allen G. Marr. Location of chlorophyll in Rhodospirillum rubrum. J. Bacteriol. 89:1402-1412. 1965.-If cells of Rhodospirillum rubrum are broken by sonic and ballistic disruption, the chlorophyll is not found in discrete cytoplasmic structures, but is located in a more extensive structure of the cell, the intracytoplasmic membrane. Direct electron microscopy of sonically disrupted cells of R. rubrum and stereo-electron microscopy of osmotically shocked cells reveal the presence of a tubular network of internal membranes originating from the periphery of the cell.

Cell Biology↗
PubMed1965

ISOLATION AND PURIFICATION OF THE INTRACYTOPLASMIC MEMBRANES OF RHODOSPIRILLUM RUBRUM.

Holt, Stanley C. (University of California, Davis), and Allen G. Marr. Isolation and purification of the intracytoplasmic membranes of Rhodospirillum rubrum. J. Bacteriol. 89:1413-1420. 1965.-When Rhodospirillum rubrum was disrupted in a French pressure cell, two colored bands were observed after density-gradient centrifugation: an upper band containing chromatophores and a lower band containing cell envelopes. A similar analysis of the pigmented components after disruption by osmotic shock revealed the presence of a third band intermediate between the upper and lower bands. Brief sonic treatment of the contents of this intermediate band produced typical chromatophores. The results establish that chromatophores are produced by fragmentation of the intracytoplasmic membrane.

Cell Membrane↗
PubMed1965

EFFECT OF LIGHT INTENSITY ON THE FORMATION OF INTRACYTOPLASMIC MEMBRANE IN RHODOSPIRILLUM RUBRUM.

Holt, Stanley C. (University of California, Davis), and Allen G. Marr. Effect of light intensity on the formation of intracytoplasmic membrane in Rhodospirillum rubrum. J. Bacteriol. 89:1421-1429. 1965.-Cells of Rhodospirillum rubrum grown at low light intensity were found to contain much more internal membrane than cells grown at high light intensity. Highly purified membranes (chromatophores) from cells grown at low to moderate light intensity had a constant content of chlorophyll. Thus, the regulation of the chlorophyll content of the cell depends upon the formation of greater or lesser amounts of membrane which has a constant concentration of chlorophyll.

Chlorophyll↗
PubMed1997

Reductive dehalogenation of halocarboxylic acids by the phototrophic genera Rhodospirillum and Rhodopseudomonas.

Type strains of the purple nonsulfur species Rhodospirillum rubrum, Rhodospirillum photometricum, and Rhodopseudomonas palustris grew phototrophically on a number of two- and three-carbon halocarboxylic acids in the presence of CO2, by reductive dehalogenation and assimilation of the resulting acid. Strains of each of these species were able to grow on chloroacetic, 2-bromopropionic, 2-chloropropionic, and 3-chloropropionic acids at a concentration of 2 mM. Only R. palustris DSM 123 was able to grow on bromoacetic acid and then only at a reduced concentration of 1 mM. R. palustris ATCC 33872 (formerly R. rutila) was unable to grow on any of the substrates tested. The ability of these organisms to utilize halocarboxylic acids indicates that they may have a significant role to play in the removal of these environmental pollutants from illuminated anaerobic habitats such as lakes, waste lagoons, sediments of ditches and ponds, mud, and moist soil.

Acetates↗