Publications
| Title | Abstract | Year Filter | PMID(sorted descending) Filter |
|---|
| effects of stearic spin-labels on the photochemical activities of chromatophores from rhodospirillum rubrum. | 1974 | 4213074 | |
| demonstration of acid-base phosphorylation in chromatophores in the presence of a k+ diffusion potential. | 1974 | 4213021 | |
| pyruvate formate lyase in rhodospirillum rubrum ha adapted to anaerobic dark conditions. | 1974 | 4212293 | |
| orthophosphate requirement for the formation of phosphoenolpyruvate from pyruvate by enzyme preparations from photosynthetic bacteria. | the formation of phosphoenolpyruvate from pyruvate and adenosine 5'-triphosphate by enzymes from photosynthetic bacteria required inorganic phosphate, thus indicating that these organisms utilize pyruvate, orthophosphate dikinase rather than phosphoenolpyruvate synthase in photosynthesis. | 1974 | 4212219 |
| n-terminal amino acid sequences of azotobacter vinelandii and rhodospirillum rubrum flavodoxins. | 1974 | 4212186 | |
| letter: comments on papers by reichert and wong. | 1974 | 4212127 | |
| occurrence of trans-phytoene in microorganisms grown in the absence of carotenogenesis inhibitors. | 1974 | 4211222 | |
| synthesis of free atp from membrane-bound atp in chromatophores of rhodospirillum rubrum. | 1974 | 4210308 | |
| chemical and physical properties of a carotenoprotein from rhodospirillum rubrum. | 1974 | 4210079 | |
| ultrastructure of rhodospirillum rubrum after freeze-etching. | 1973 | 4210026 | |
| aliphatic alcohols and bacterial motile behavior. | 1974 | 4209798 | |
| bacteriocinogeny in the athiorhodaceae. | 1974 | 4209388 | |
| [photoinduced absorption of hydrophobic penetrating anions by rhodospirillum rubrum non-sulfur purple bacteria]. | 1973 | 4209366 | |
| photochemical disproportionation of sulfur into sulfide and sulfate by chlorobium limicola forma thiosulfatophilum. | 1974 | 4209228 | |
| [formation of different forms of hydrogenases in rhodospirillum rubrum depending on the growing conditions]. | 1973 | 4208935 | |
| [composition of nonconjugated pteridines in phototrophic bacteria]. | 1974 | 4208903 | |
| d-ribulose 1,5-diphosphate carboxylase from rhodospirillum rubrum. ii. quaternary structure, composition, catalytic, and immunological properties. | 1974 | 4208662 | |
| d-ribulose 1,5-diphosphate carboxylase from rhodospirillum rubrum. i. levels, purification, and effects of metallic ions. | 1974 | 4208661 | |
| acid-base indicator for the measurement of rapid changes in hydrogen ion concentration. | 1972 | 4206743 | |
| [comparative study of nitrogen fixation in purple bacteria]. | 1973 | 4205730 | |
| competition between pi and ph indicators in photosynthetic atp formation in chromatophores of rhodospirillum rubrum. | 1973 | 4205462 | |
| studies on ion transport in cells of photosynthetic bacteria. 3. the influence of uncouplers on hydrogen ion change. | 1973 | 4205460 | |
| studies on ion transport in cells of photosynthetic bacteria. ii. analysis of reversed hydrogen ion change. | 1973 | 4205459 | |
| studies on ion transport in cells of photosynthetic bacteria. i. the key role of anions in determining the direction and magnitude of hydrogen ion flux. | 1973 | 4205458 | |
| [a comparative study of photooxidation of chlorophyll analogs in an aqueous solution of detergents]. | 1973 | 4204958 | |
| comparison of phototrap complexes from chromatophores of rhodospirillum rubrum, rhodopseudomonas spheroides, and the r-26 mutant of rhodopseudomonas spheroides. | 1973 | 4204253 | |
| control of magnesium-protoporphyrin chelatase activity in rhodopseudomonas spheroides. role of light, oxygen, and electron and energy transfer. | 1. magnesium-protoporphyrin chelatase activity, previously shown in whole cells of rhodopseudomonas spheroides, could not be demonstrated in cell-free extracts prepared in different ways, although spheroplasts retained moderate activity. slight activity was detected also in whole cells of rhodospirillum rubrum. 2. the effects on the activity of the enzyme of inhibitors of electron and energy transfer were studied in whole cells of rps. spheroides. amytal, rotenone, azide and cyanide inhibited at ... | 1973 | 4202754 |
| monomolecular films of bacteriochlorophyll and derivatives at an air-water interface: surface and spectral properties. | 1973 | 4201590 | |
| laser flash photolysis studies of chlorin and porphyrin systems. i. energetics of the triplet state of bacteriochlorophyll. | 1973 | 4201440 | |
| the pathway of carbon dioxide assimilation in rhodospirillum rubrum grown in turbidostat continuous-flow culture. | 1973 | 4201020 | |
| homoserine dehydrogenase of rhodospirillum rubrum. enzyme polymerization in the presence and absence of threonine. | 1973 | 4200889 | |
| growth properties of rhodospirillum rubrum mutants and fermentation of pyruvate in anaerobic, dart conditions. | mutant c and g1 were obtained earlier from rhodospirillum rubrum s(1) during growth in the dark under strict anaerobic conditions in medium containing sodium pyruvate. mutant c and mutant g1 grew in the dark with generation times of 5.8 h and 4.6 h, respectively. mutant c cells grew equally well when switched between anaerobic (dark or light) or aerobic, dark conditions. mutant g1 cells grew only in the dark (anaerobic or aerobic conditions), but a fraction of cells in anaerobic, dark cultures g ... | 1973 | 4200859 |
| effect of low-intensity light on growth response and bacteriochlorophyll concentration in rhodospirillum rubrum mutant c. | photosynthesizing cells of rhodospirillum rubrum mutant c underwent adaptation for growth in low-light conditions. during adaptation there was a transitory increase in the generation time and the bacteriochlorophyll a content of the cells. | 1973 | 4200847 |
| the bacteriochlorophyll absorption band shifts linked with the energy state of photosynthetic bacteria membranes. | 1973 | 4200406 | |
| atomic coordinates for ferricytochrome c2 of rhodospirillum rubrum. | 1973 | 4200400 | |
| circular dichroism studies on protohemoproteins. 3. cytochrome b5 from rabbit liver microsomes, and cytochrome b-557.5 from rhodospirillum rubrum. | 1973 | 4198544 | |
| role of bound adp in photosynthetic atp formation by chromatophores from rhodospirillum rubrum. | 1972 | 4198252 | |
| [occurrence of bacteriochlorophyll a p and a gin strains of all species of the rhodospirillaceae]. | 1973 | 4197122 | |
| [alcohol components of bacteriophyll a from rhodospirillum rubrum]. | 1973 | 4196489 | |
| fluorescence polarization and pigment orientation in photosynthetic bacteria. | 1973 | 4196189 | |
| fat metabolism in higher plants. lvi. distribution and nature of biotin in chloroplasts of different plant species. | 1973 | 4196182 | |
| [the bacteriochlorophyll content and protein composition of thylakoids of rhodospirillum rubrum during morphogenesis of the photosynthetic apparatus]. | 1969 | 4194589 | |
| ctothiorhodospira halophila: a new species ofthe genus ectothiorhodospira. | 1969 | 4192367 | |
| [the influence of the partial pressure of oxygen and of the antibiotics actinomycin and puromycin on the growth, the bacteriochlorophyll synthesis, and the morphogenesis of thylakoids in dark cultures of rhodospirillum rubrum]. | 1967 | 4173527 | |
| [nitrate utilization by purple bacteria]. | 1974 | 4155788 | |
| a soluble transhydrogenase enzyme from rhodospirillum rubrum chromatophores. | 1974 | 4155373 | |
| [lipopolysaccharides from rhodospirillaceae: composition and taxonomic relevance]. | 1974 | 4154665 | |
| redox potentiometry in mitochondrial and photosynthetic bioenergetics. | 1974 | 4154105 | |
| light-dependent synthesis of glutamate in rhodospirillum rubrum. physiological evidence for ammonia assimilation via the glutamine synthetase and glutamine: 2-oxoglutarate amino-transferase system. | 1974 | 4151925 | |
| [membrane potential in the chromatophores of rhodospirillum rubrum conditioned by a transhydrogenase reaction]. | 1974 | 4150987 | |
| two different nadh dehydrogenases in respiration of rhodospirillum rubrum chromatophores. | 1973 | 4149985 | |
| membrane differentiation in phototrophically growing rhodospirillum rubrum during transition from low to high light intensity. | 1973 | 4148662 | |
| spectrophotometric studies of the mechanism of photosynthesis. | 1970 | 4146947 | |
| immunological studies on function of nadh: quinone oxidoreductase in electron transport system of chromatophores from rhodospirillum rubrum. | 1973 | 4146750 | |
| immunochemical studies on function of nadh: hemeprotein oxidoreductase in electron transport system of chromatophores from rhodospirillum rubrum. | 1973 | 4146749 | |
| [photophosphorylation and binding of phosphates to chromatophores in rhodospirillum rubrum]. | 1972 | 4145605 | |
| [substrate utilization and bacteriochlorophyll synthesis by rhodospirillum rubrum under anaerobic conditions in the dark. i. dependence of bacteriochlorophyl synthesis on substrate concentration and electron acceptor]. | 1972 | 4145604 | |
| transhydrogenase-induced responses of carotenoids, bacteriochlorophyll and penetrating anions in rhodospirillum rubrum chromatophores. | 1973 | 4145457 | |
| the influence of 2-hydroxybiphenyl on membranes of rhodospirillum rubrum. | 1973 | 4130016 | |
| protein components of bacterial photosynthetic membranes. | 1972 | 4115110 | |
| the fine structure of "resting bodies" of bdellovibrio sp. strain w developed in rhodospirillum rubrum. | 1972 | 4110832 | |
| anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations. | 1970 | 4100801 | |
| the mechanism of the c-13(3) esterification step in the biosynthesis of bacteriochlorophyll a. | 5-aminolaevulinate labelled with 18o at its c-1 carboxy oxygen atoms was prepared and incorporated into bacteriochlorophyll aphytyl of rhodopseudomonas sphaeroides and bacteriochlorophyll ageranylgeranyl of rhodospirillum rubrum. the biosynthetic samples of the bacteriochlorophylls were separately processed to obtain their isoprenyl alcohol components from the c-17(3) ester linkages and methanol from the c-13(3) methoxycarbonyl group. methods were developed for the quantification of the isotopic ... | 1985 | 4018085 |
| the amino acid sequence of a high-redox-potential ferredoxin from the purple phototrophic bacterium, rhodospirillum tenue strain 2761. | the 61-residue amino acid sequence of rhodospirillum tenue, strain 2761, high-redox-potential ferredoxin (hipip) is gtnaamrkafnyqdtakngkcsgcaqfvpgasptaaggckvipgdneiapggycdafivkk. it differs from that of r. tenue strain 3761 by 16 amino acid substitutions plus two single-residue deletions. this 26% sequence difference is similar to that observed among separate species of chromatiaceae such as chromatium vinosum, c. gracile, and thiocapsa roseopersicina, and is suprising because there are no disti ... | 1985 | 4004266 |
| new crystal forms of ribulose-1,5-bisphosphate carboxylase/oxygenase from rhodospirillum rubrum. | three crystal forms of the dimeric form of the enzyme ribulose-1,5-bisphosphate carboxylase from the photosynthetic bacterium rhodospirillum rubrum have been obtained from the gene product expressed in escherichia coli. form a crystals formed from the quaternary complex comprising enzyme-activator carbamate-mg2+-2'-carboxyarabinitol-1,5-bisphosphate are shown here to be devoid of ligands. in contrast, crystals of the quaternary complex formed with the hexadecameric l8s8 enzyme from spinach conta ... | 1986 | 3959081 |
| crystallization and preliminary analysis of crystals of high potential iron-sulfur protein from rhodospirillum tenue. | large single crystals of the high potential iron-sulfur protein isolated from rhodospirillum tenue strain 3761 have been obtained. they belong to the space group p2(1) with unit cell dimensions of a = 36.7 a, b = 52.6 a, c = 27.6 a, and beta = 90.8 degrees. there are two molecules in the asymmetric unit. based on oscillation photographs, the crystals diffract to at least 1.6 a resolution. they are stable in the x-ray beam and appear suitable for a high resolution x-ray structure analysis. | 1986 | 3949809 |
| comparative efficiency of primary light conversion in photosynthetic bacteria rhodospirillum rubrum and rhodopseudomonas viridis. | 1985 | 3939722 | |
| isolation, characterization, and comparison of a ubiquitous pigment-protein complex consisting of a reaction center and light-harvesting bacteriochlorophyll proteins present in purple photosynthetic bacteria. | protein complexes (photochemical reaction complex; pr complex) bound to both light-harvesting bacteriochlorophyll-1 (lh-bchl-1) and reaction center bchl (rc-bchl) were purified from rhodospirillum rubrum (wild and carotenoid-less), rhodopseudomonas sphaeroides (wild), and chromatium vinosum (wild). another protein complex (lh-2 complex) bound to lh-bchl-2 was also purified from rps. sphaeroides. the bacteria were grown in the presence of a [14c]amino acid mixture. the purification procedure incl ... | 1985 | 3937841 |
| membrane topology of light-harvesting protein b870-alpha of rhodospirillum rubrum g-9+. amino acid residues in contact with the lipid bilayer as inferred from labeling with photogenerated carbenes. | the amino acid residues of the light-harvesting protein b870-alpha of rhodospirillum rubrum g-9+ that in the chromatophore membranes are in contact with the lipid phase were identified by hydrophobic photolabeling. three reagents have been used which all contained the trifluoromethyldiazirinylphenyl group as a photo-sensitive precursor of a carbene but which otherwise differed in shape, molecular structure, and in the way they interact with membranes. 3-trifluoromethyl-3-(m-[125i]iodophenyl)diaz ... | 1985 | 3934175 |
| crystallization of the activated ternary complex of ribulose-1,5-bisphosphate carboxylase-oxygenase isolated from rhodospirillum rubrum and from an escherichia coli clone. | ribulose-1,5-bisphosphate carboxylase-oxygenase was purified from the photosynthetic bacterium rhodospirillum rubrum as well as from an escherichia coli clone overproducing the enzyme. although the latter enzyme contains 25 additional amino acid residues at the n terminus, both preparations yielded isomorphous tetragonal, bipyramidal crystals of the ternary complex of the enzyme with co2 and mg2+. crystallization is sensitive to variation in ph and to the addition of the transition state analog, ... | 1985 | 3932659 |
| ionization constants of two active-site lysyl epsilon-amino groups of ribulosebisphosphate carboxylase/oxygenase. | trinitrobenzene sulfonate rapidly inactivates ribulosebisphosphate carboxylase/oxygenase from both spinach and rhodospirillum rubrum. with large molar excesses of the reagent, the reactions obey pseudo-first order kinetics and the rates of inactivations are directly proportional to the concentrations of trinitrobenzene sulfonate; thus, there is no indication of reversible complexation of reagent with enzyme. saturating levels of the competitive inhibitor 2-carboxyribitol 1,5-bisphosphate reduce ... | 1985 | 3932347 |
| distribution of multicopy single-stranded dna among myxobacteria and related species. | multicopy single-stranded dna (msdna) is a short single-stranded linear dna originally discovered in myxococcus xanthus and subsequently found in stigmatella aurantiaca. it exists at an estimated 500 to 700 copies per chromosome (t. yee, t. furuichi, s. inouye, and m. inouye, cell 38:203-209, 1984). we found msdna in other myxobacteria, including myxococcus coralloides, cystobacter violaceus, cystobacter ferrugineus (cbfe17), nannocystis exedens, and nine independently isolated strains of m. xan ... | 1985 | 3932332 |
| polyamines in photosynthetic eubacteria and extreme-halophilic archaebacteria. | qualitative and quantitative determinations of polyamines have been done in 4 photosynthetic eubacteria and 6 extreme-halophilic archaebacteria. for comparison, 5 moderate-halophilic eubacteria were also analyzed to determine their polyamine contents. not only putrescine and spermidine but also homospermidine were found in the photosynthetic eubacteria, especially in the n2-fixing species, rhodospirillum and chromatium. norspermidine, norspermine, and spermine were not detected in the phototroph ... | 1985 | 3928615 |
| influence of ph, o2, and temperature on the absorption properties of the secondary light-harvesting antenna in members of the family rhodospirillaceae. | in some rhodospirillaceae, the primary light-harvesting (lh i) antenna absorbs near-infrared light around 870 nm, whereas lh ii (holochrome b800-860) has a major absorption band between 850 and 860 nm (b860) and a minor absorbancy around 800 nm (b800). results show that, unlike lh i, holochrome b800-860 (lh ii) exhibits unstable light absorption properties in whole cells. this was observed in rhodopseudomonas capsulata grown anaerobically in light in weakly buffered carbohydrate medium; cultures ... | 1985 | 3928601 |
| carbon isotope effect on carboxylation of ribulose bisphosphate catalyzed by ribulosebisphosphate carboxylase from rhodospirillum rubrum. | the carbon isotope effect at co2 has been measured in the carboxylation of ribulose 1,5-bisphosphate by the ribulosebisphosphate carboxylase from rhodospirillum rubrum. the isotope effect is obtained by comparing the isotopic composition of carbon 1 of the 3-phosphoglyceric acid formed in the reaction with that of the carbon dioxide source. a correction is made for carbon 1 of 3-phosphoglyceric acid which arises from carbon 3 of the starting ribulose bisphosphate. the isotope effect is k12/k13 = ... | 1985 | 3924094 |
| covalent modification of the iron protein of nitrogenase from rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue. | nitrogenase in rhodospirillum rubrum is inactivated in vivo by the covalent modification of the fe protein with a nucleotide. the preparation of two modified peptides derived from proteolytic digestion of the inactive fe protein is described. the modifying group is shown to be adenosine diphosphoribose, linked through the terminal ribose to a guanidino nitrogen of arginine. the structural features were established by using proton and phosphorus nmr, positive- and negative-ion fast atom bombardme ... | 1985 | 3923473 |
| regulation of nitrogen fixation in rhodospirillum rubrum grown under dark, fermentative conditions. | rhodospirillum rubrum was shown to grow fermentatively on fructose with n2 as a nitrogen source. the nitrogenase activity of these cells was regulated by the nh4+ switch-off/switch-on mechanism in a manner identical to that for photosynthetically grown cells. in vitro, the inactive nitrogenase fe protein from fermenting cells was reactivated by an endogenous membrane-bound, mn2+-dependent activating enzyme that was interchangeable with the activating enzyme isolated from photosynthetic membranes ... | 1985 | 3922950 |
| purification and properties of the heat-released nucleotide-modifying group from the inactive iron protein of nitrogenase from rhodospirillum rubrum. | nitrogenase in rhodospirillum rubrum is regulated in vivo by the covalent modification of the fe protein. this paper reports the isolation, purification, and properties of the modifying group that has been heat released from the fe protein. the molecule is isolated from the heated mixture by binding to a boronate affinity column. purification is achieved on an ion-exchange high-performance liquid chromatography column. structural properties of the molecule have been investigated by using proton ... | 1985 | 3922413 |
| evidence of tyrosine kinase activity in the photosynthetic bacterium rhodospirillum rubrum. | the photosynthetic bacterium rohodospirillum rubrum evidenced tyrosine protein phosphorylation under photoautotrophic conditions in the presence of [32p]pi. the stability to alkaline treatment of the [32p] bound to the cell-free extract proteins suggested that tyrosine residues were carrying the labelling. one- and two-dimensional high voltage paper electrophoresis analysis revealed that such extracts do contain [32p]-phosphotyrosine residues. furthermore, the association of alkali stable [32p] ... | 1985 | 3919714 |
| partition kinetics of ribulose-1,5-bisphosphate carboxylase from rhodospirillum rubrum. | when the enzymatically generated intermediate 2-carboxy-3-keto-d-arabinitol-1,5-bisphosphate (ii) was used as a substrate with fresh enzyme, 70% reacted to produce 3-phosphoglycerate (3pga). when a reaction mixture of enzyme plus [1-32p]ribulose 1,5-bisphosphate (rubp) was quenched in the steady state with the tightly bound inhibitor 2-carboxyarabinitol-1,5-bisphosphate, 30% of the enzyme-bound species was released as 3pga and 70% as rubp. the major source for this partition was the ternary subs ... | 1985 | 3918036 |
| dna-directed in vitro synthesis and assembly of the form ii d-ribulose-1,5-bisphosphate carboxylase/oxygenase from rhodopseudomonas sphaeroides. | a biochemical analysis of the in vitro assembly of the form ii ribulose-1,5-bisphosphate carboxylase/oxygenase from rhodopseudomonas sphaeroides after transcription and translation from cloned dna is presented. the predominant enzymatically active oligomeric forms of the in vitro-synthesized and -assembled ribulose-1,5-bisphosphate carboxylase are tetramers and hexamers. assembly of the monomeric subunits to form active enzyme appears to be dependent on the presence of a minimum number of subuni ... | 1985 | 3918003 |
| the light-harvesting polypeptides of rhodopseudomonas viridis. the complete amino-acid sequences of b1015-alpha, b1015-beta and b1015-gamma. | three low molecular mass polypeptides have been isolated by using the technique of organic solvent extraction of thylakoid membranes or whole cells from rhodopseudomonas viridis. their primary structures were determined by long liquid phase sequencer runs, combined with the isolation and sequence analysis of the c-terminal o-iodosobenzoic acid fragment and carboxypeptidase degradation. the polypeptide which consists of 58 amino-acids and is 46% homologous to the antenna polypeptide b880-alpha fr ... | 1985 | 3890891 |
| large-scale preparation of ribulosebisphosphate carboxylase from a recombinant system in escherichia coli characterized by extreme plasmid instability. | an ampicillin-resistant, reca- strain of escherichia coli (hb101) harboring the multicopy pbr322 plasmid containing the structural gene for ribulosebisphosphate carboxylase from rhodospirillum rubrum was used to prepare large quantities of the carboxylase protein. this recombinant system was characterized by extreme plasmid instability, which resulted in part from the 1.7-fold faster growth rate of plasmid-free cells and in part from very rapid rates of plasmid segregation. the plasmid-containin ... | 1985 | 3890745 |
| 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 associa ... | 1985 | 3874866 |
| purification and properties of the nitrogenase of azospirillum amazonense. | the nitrogenase of the free-living, microaerobic, n2-fixing bacterium azospirillum amazonense (strain y1) was purified by chromatography on deae-52 cellulose, by heat treatment, and by preparative polyacrylamide gel electrophoresis. the specific nitrogenase activities were 2,400 nmol of c2h4 formed per min per mg of protein for dinitrogenase (mofe protein) and 1,800 nmol of c2h4 formed per min per mg of protein for dinitrogenase reductase (fe protein). the mofe protein was composed of a minimum ... | 1985 | 3864779 |
| characterization of an active-site peptide modified by glyoxylate and pyridoxal phosphate from spinach ribulosebisphosphate carboxylase/oxygenase. | activated ribulosebisphosphate carboxylase/oxygenase from spinach was treated with glyoxylate plus or minus the transition-state analog, carboxyarabinitol bisphosphate, or the inactive enzyme with pyridoxal phosphate plus or minus the substrate, ribulose bisphosphate. covalently modified adducts with glyoxylate or pyridoxal phosphate were formed following reduction with sodium borohydride. the derivatized enzymes were carboxymethylated and digested with trypsin; the labeled peptides which were u ... | 1985 | 3860189 |
| regulation of nitrogenase activity by covalent modification in chromatium vinosum. | nitrogenase in chromatium vinosum was rapidly, but reversibly inhibited by nh4+. activity of the fe protein component of nitrogenase required both mn2+ and activating enzyme. activating enzyme from rhodospirillum rubrum could replace chromatium chromatophores in activating the chromatium fe protein, and conversely, a protein fraction prepared from chromatium chromatophores was effective in activating r. rubrum fe protein. inactive chromatium fe protein contained a peptide covalently modified by ... | 1985 | 3857878 |
| the nature of l8 and l8s8 forms of ribulose bisphosphate carboxylase/oxygenase from chromatium vinosum. | l8 and l8s8 forms of ribulose bisphosphate carboxylase/oxygenase (rubisco) have been prepared from chromatium vinosum by the extremely mild method of centrifugal fractionation. only the l8s8 form is detectable in crude extracts of this organism. both forms show immunological identify in double diffusion studies using antibody to l subunits of the l8s8 form. l subunits from both l8 and l8s8 enzymes are identical by the criteria of peptides observed after limited proteolysis and n-terminal sequenc ... | 1987 | 3579306 |
| production of long-chain alcohols by yeasts. | fourteen yeast strains from six genera were analysed for the presence of long-chain alcohols. six strains from three genera contained long-chain alcohols, highest levels being found in candida albicans. the alcohols were identified and determined by tlc, glc and glc-ms. the major long-chain alcohols synthesized by these organisms were saturated, primary alcohols with c14, c16 or c18 chain length. unsaturated long-chain alcohols were not detected. in all strains that produced long-chain alcohols, ... | 1987 | 3327916 |
| essentiality of lys-329 of ribulose-1,5-bisphosphate carboxylase/oxygenase from rhodospirillum rubrum as demonstrated by site-directed mutagenesis. | the unusual chemical properties of active-site lys-329 of ribulose bisphosphate carboxylase/oxygenase from rhodospirillum rubrum have suggested that this residue is required for catalysis. to test this postulate lys-329 was replaced with glycine, serine, alanine, cysteine, arginine, glutamic acid or glutamine by site-directed mutagenesis. these single amino acid substitutions do not appear to induce major conformational changes because (i) intersubunit interactions are unperturbed in that the pu ... | 1988 | 3151016 |
| real time computer tracking of free-swimming and tethered rotating cells. | a computerized image processing system has been developed that tracks individual free-swimming cells and rotating bacterial cell bodies tethered by their flagella in real time. free-swimming bacteria of rhodobacter sphaeroides, rhodospirullum rubrum, and salmonella typhimurium have been tracked swimming at speeds from 0 to over 120 microns s-1. a high level of discrimination is exerted against noncellular objects, allowing analysis of stopped as well as moving cells. this enabled detection of bo ... | 1988 | 3149876 |
| oxygen-dependent inactivation of ribulose 1,5-bisphosphate carboxylase/oxygenase in crude extracts of rhodospirillum rubrum and establishment of a model inactivation system with purified enzyme. | ribulose 1,5-bisphosphate (rubp) carboxylase/oxygenase (rubpc/o) was inactivated in crude extracts of rhodospirillum rubrum under atmospheric levels of oxygen; no inactivation occurred under an atmosphere of argon. rubp carboxylase activity did not decrease in dialyzed extracts, indicating that a dialyzable factor was required for inactivation. the inactivation was inhibited by catalase. purified rubpc/o is relatively oxygen stable, as no loss of activity was observed after 4 h under an oxygen a ... | 1988 | 3142847 |
| oxygen regulation of ribulose 1,5-bisphosphate carboxylase activity in rhodospirillum rubrum. | the carboxylase activity of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubpc/o) decreased when an anaerobic culture of rhodospirillum rubrum was exposed to atmospheric levels of oxygen. from 70 to 80% of the activity was lost within 12 to 24 h. inactivation was apparent when the enzyme was assayed in situ (in whole cells) and when activity was measured in dialyzed crude extracts. the quantity of enzyme protein, as estimated from sodium dodecyl sulfate-polyacrylamide gels or as quantified i ... | 1988 | 3142846 |
| purification and properties of dinitrogenase reductase adp-ribosyltransferase from the photosynthetic bacterium rhodospirillum rubrum. | the enzyme that catalyzes the adp-ribosylation and concomitant inactivation of dinitrogenase reductase in rhodospirillum rubrum has been purified greater than 19,000-fold to near homogeneity. we propose dinitrogenase reductase adp-ribosyltransferase (drat) as the working name for the enzyme. drat activity is stabilized by nacl and adp. the enzyme is a monomer with a molecular mass of 30 kda and is a different polypeptide than dinitrogenase reductase activating glycohydrolase. nad (km = 2 mm), et ... | 1988 | 3141411 |
| malate dehydrogenases in phototrophic purple bacteria. thermal stability, amino acid composition and immunological properties. | purified malate dehydrogenases from four species of non-sulphur purple phototrophic bacteria were examined for their heat-stability, amino acid composition and antigenic relationships. malate dehydrogenase from rhodospirillum rubrum, rhodobacter capsulatus and rhodomicrobium vannielii (which are all tetrameric proteins) had an unusually high glycine content, but the enzyme from rhodocyclus purpureus (which is a dimer) did not. r. rubrum malate dehydrogenase was extremely heat-stable relative to ... | 1988 | 3137931 |
| ammonia switch-off of nitrogenase from rhodobacter sphaeroides and methylosinus trichosporium: no evidence for fe protein modification. | in vivo switch-off of nitrogenase activity by nh4+ is a reversible process in rhodobacter sphaeroides and methylosinus trichosporium ob3b. the same pattern of switch-off in rhodospirillum rubrum is explained by adp-ribosylation of one of the fe protein subunits, however, no evidence of covalent modification could be found in the subunits from either r. sphaeroides or m. trichosporium. fe protein subunits from these organisms showed no variant behaviour on sds-page, nor were they 32p-labeled foll ... | 1988 | 3136733 |
| structural and evolutionary aspects of the key enzymes in photorespiration; rubisco and glycolate oxidase. | 1987 | 3135980 | |
| reconstitution of the b873 light-harvesting complex of rhodospirillum rubrum from the separately isolated alpha- and beta-polypeptides and bacteriochlorophyll a. | the light-harvesting complex of rhodospirillum rubrum was reversibly dissociated into its component parts: bacteriochlorophyll and two 6-kilodalton polypeptides. the dissociation of the complex by n-octyl beta-d-glucopyranoside was accompanied by a shift of the absorbance maximum from 873 to 820 nm (a stable intermediate form) and finally to 777 nm. in the latter state, bacteriochlorophyll was shown to be free from the protein. complexes absorbing at 820 and 873 nm could be re-formed from the fu ... | 1988 | 3135833 |
| adp-ribosylation of dinitrogenase reductase from clostridium pasteurianum prevents its inhibition of nitrogenase from azotobacter vinelandii. | the effect of adp-ribosylation of dinitrogenase reductase on its binding to dinitrogenase was investigated. dinitrogenase reductase from clostridium pasteurianum (cp2) was a substrate for the adp-ribosyltransferase and the dinitrogenase-reductase-activating glycohydrolase from rhodospirillum rubrum. adp-ribosylation inactivated cp2 and prevented its formation of a tight complex with dinitrogenase from azotobacter vinelandii (av1). the complex between cp2 and av1 could not be adp-ribosylated once ... | 1988 | 3135803 |
| tertiary structure of plant rubisco: domains and their contacts. | the three-dimensional structure of ribulose-1,5-biphosphate carboxylase-oxygenase (rubisco), has been determined at 2.6 a resolution. this enzyme initiates photosynthesis by combining carbon dioxide with ribulose bisphosphate to form two molecules of 3-phosphoglycerate. in plants, rubisco is built from eight large (l) and eight small (s) polypeptide chains, or subunits. both s chains and the nh2-terminal domain (n) of l are antiparallel beta, "open-face-sandwich" domains with four-stranded beta ... | 1988 | 3133767 |