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At least 217 records · Page 12Linked to original sources
PubMed1991

Velocity changes, long runs, and reversals in the Chromatium minus swimming response.

The velocity, run time, path curvature, and reorientation angle of Chromatium minus were measured as a function of light intensity, temperature, viscosity, osmotic pressure, and hydrogen sulfide concentration. C. minus changed both velocity and run time. Velocity decreased with increasing light intensity in sulfide-depleted cultures and increased in sulfide-replete cultures. The addition of sulfide to cultures grown at low light intensity (10 microeinsteins m-2 s-1) caused mean run times to increase from 10.5 to 20.6 s. The addition of sulfide to cultures grown at high light intensity (100 microeinsteins m-2 s-1) caused mean run times to decrease from 15.3 to 7.7 s. These changes were maintained for up to an hour and indicate that at least some members of the family Chromatiaceae simultaneously modulate velocity and turning frequency for extended periods as part of normal taxis.

Cell Movement↗
PubMed1993

Cloning, characterization, and functional expression in Escherichia coli of chaperonin (groESL) genes from the phototrophic sulfur bacterium Chromatium vinosum.

A recombinant lambda phage which was able to propagate in groE mutants of Escherichia coli was isolated from a Chromatium vinosum genomic DNA library. A 4-kbp SalI DNA fragment, isolated from this phage and subcloned in plasmid vectors, carried the C. vinosum genes that allowed lambda growth in these mutants. Sequencing of this fragment indicated the presence of two open reading frames encoding polypeptides of 97 and 544 amino acids, respectively, which showed high similarity to the molecular chaperones GroES and GroEL, respectively, from several eubacteria and eukaryotic organelles. Expression of the cloned C. vinosum groESL genes in E. coli was greatly enhanced when the cells were transferred to growth temperatures that induce the heat shock response in this host. Coexpression in E. coli of C. vinosum groESL genes and the cloned ribulose bisphosphate carboxylase/oxygenase genes from different phototrophic bacteria resulted in an enhanced assembly of the latter enzymes. These results indicate that the cloned DNA fragment encodes C. vinosum chaperonins, which serve in the assembly process of oligomeric proteins. Phylogenic analysis indicates a close relationship between C. vinosum chaperonins and their homologs present in pathogenic species of the gamma subdivision of the eubacterial division Proteobacteria.

Amino Acid Sequence↗
PubMed1967

Effect of oxygen on viability and substrate utilization in Chromatium.

Chromatium D can be exposed to oxygen for prolonged periods without any loss in motility or viability. Oxygen did not affect the rate of thiosulfate disappearance from the media, the oxidation of the inner sulfur atom of thiosulfate to sulfate, or the conversion of the outer sulfur atom of thiosulfate to intracellular sulfur, but it did inhibit the oxidation of intracellular sulfur to sulfate. Oxygen partially inhibited the uptake of pyruvate from the medium, but had little effect on the uptake of acetate. The distribution of label from pyruvate-2-(14)C into various cell fractions under aerobic conditions differed only slightly from that obtained under anaerobic conditions. Cells utilizing acetate-2-(14)C aerobically converted the majority of the metabolized acetate into a cell fraction with the solubility characteristics of poly-beta-hydroxybutyric acid, whereas under anaerobic conditions the acetate was distributed throughout the other cell fractions. Oxygen completely prevented the synthesis of bacteriochlorophyll.

Acetates↗
PubMed1967

Changes in adenine nucleotides of intact Chromatium D produced by illumination.

The total adenine nucleotide content of suspensions of Chromatium D averaged 14 nmoles/mg of dry weight. Of this, one-third to one-half was adenosine triphosphate (ATP), even in suspensions incubated in darkness. Illumination with high intensities caused a rise in ATP and a drop mainly in adenosine diphosphate, the new steady state being reached in 5 to 15 sec at room temperature. The dark steady state was re-established 15 to 30 sec after returning the suspensions to darkness. The rates of these changes were little affected by the presence of electron donors or CO(2), though their magnitude was reduced when substrates were added to starved suspensions. At limiting light intensities, complex kinetics characterized the transition from both dark to light and light to dark, and, at lower light intensities, more ATP was produced in suspensions supplemented with electron donors than in starved cells. The results show that photophosphorylation accompanying cyclic electron flow occurred in intact cells, and suggest that noncyclic phosphorylation can also occur.

Adenine Nucleotides↗
PubMed1968

Effect of thiol-binding reagents on the metabolism of Chromatium D.

Thiosulfate, intracellular sulfur, and acetate utilization by Chromatium D were inhibited by iodoacetamide, N-ethylmaleimide (NEM), p-hydroxymercuribenzoate (CMB), and HgCl(2). Pyruvate, sulfide, and sulfite utilization were insensitive to iodoacetamide, and were less sensitive to NEM, CMB, and HgCl(2) than thiosulfate, intracellular sulfur, and acetate utilization. The effect of the thiol-binding reagents on cell viability was dependent upon the method of exposure; cells exposed to the thiol-binding reagents in the presence of thiosulfate were protected from the killing action of these agents, but not from their inhibitory effect. Although the inhibitory effects of the thiol-binding reagents could, in some cases, be attributed to their effect on viability, they were inhibitory under conditions where viability was unaffected. The most straightforward results were obtained with iodoacetamide, which revealed a sharp separation in sensitivities between the systems tested but had no effect on cell viability. The results are consistent with the hypothesis that thiols are involved in thiosulfate, intracellular sulfur, and acetate utilization.

Acetates↗
PubMed1969

Separation and identification of the polar lipids of Chromatium strain D.

The polar lipids of the autotrophically grown, obligately anaerobic, photosynthetic bacterium Chromatium strain D were separated by paper chromatography. Four major phospholipids were identified: lysophosphatidylethanolamine, phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin. In addition, three glycolipids were observed and characterized, namely, monoglucosyldiglyceride, which is found in other biological systems, and (mannosyl, glucosyl)-diglyceride and (dimannosyl, glucosyl)-diglyceride, which heretofore have not been observed in nature.

Autoradiography↗
PubMedDate not supplied

Cytochromes and anaerobic sulfide oxidation in the purple sulfur bacterium Chromatium warmingii.

Two soluble acidic c-type cytochromes--c' and c-552--were isolated by ion exchange chromatography, gel filtration and ammonium sulfate fractionation. Cytochrome c' is a high-spin cytochrome with maxima at 399 nm, 490 nm, and 634 nm in the oxidized form and at 550 nm, 425 nm and a characteristic shoulder at 434 nm in the reduced state. The best purity index obtained (A280/A399) was 0.35. Cytochrome c' is autoxidizable, has a molecular weight of 12000 (estimated by sodium dodecylsulfate electrophoresis), a midpoint redoxpotential of +10 mV and an isoelectric point at pH 4.0. The reduced cytochrome c' reacts with carbon monoxide. The reaction is reversible. Cytochrome c-552 shows maxima at 552 nm, 523 nm and 417 nm in the reduced form and at 408 nm in the oxidized state. The best purity index obtained (A280/A408) was 0.94. Cytochrome c-552 has a molecular weight of 30000 and an isoelectric point between pH 4.3 and 5.0. Chromatium warmingii also contains a membrane-bound cytochrome c-552. During anaerobic sulfide oxidation, elemental sulfur and sulfate were formed at the same time. When all sulfide was consumed by the cells, the remaining intracellular elemental sulfur was further oxidized to sulfate.

Anaerobiosis↗
PubMedDate not supplied

Molecular properties of high potential iron sulfur protein of Chromatium warmingii.

High potential iron sulfur protein (HIPIP) of the purple sulfur bacterium Chromatium warmingii was purified to homogeneity by ion exchange chromatography, gel filtration and ammonium sulfate fractionation. The acidic protein was isolated in the reduced form. The best purity index (A280/A388) obtained was 2.52, and 3.8 mumol of the protein was isolated out of 100 g wet cell material. The molecular weights estimated by sodium dodecylsulfate polyacrylamide gel electrophoresis and gel filtration through Sephacryl S-200 were 8900 and 10 500, respectively. The protein has an isoelectric point at pH 3.6 for the reduced form and at pH 3.8 for the oxidized form, and a midpoint redox potential of +355 mV. One mol of HIPIP contains 4 mol nonheme iron and 4 mol acid-labile sulfur.

Bacterial Proteins↗
PubMedDate not supplied

[The activity of the carbon metabolism enzymes in Chromatium minutissimum after long-term preservation].

The activity of the enzymes of the tricarboxylic acid cycle and glyoxylate shunt, as well as of some enzymes involved in carbohydrate metabolism, were determined in the purple sulfur bacterium Chromatium minutissimum, either maintained by subculturing in liquid medium or stored in the lyophilized state for 36 years. In cultures stored in the lyophilized state, the activities of the key enzymes of the tricarboxylic acid cycle, glyoxylate shunt, and Embden-Meyerhof-Parnas pathway were higher, whereas the activities of glucose-6-phosphate dehydrogenase, pyruvate kinase, and ribulose bisphosphate carboxylase were somewhat lower than in cultures maintained by regular transfers.

Carbon↗
PubMed1975

Crystallographic structure refinement of Chromatium high potential iron protein at two Angstroms resolution.

The structure of Chromatium high potential iron protein (HiPIP) has been refined by semiautomatic Fo-Fc (observed minus calculated structure amplitude Fourier methods to a convential R index, R=sum of the absolute value of Fo-Fc divided by the sum of Fo, of 24.7% for a model in which bond distances and angles are constrained to standard values. Bond length and angle constraints were applied only intermittenly during the computations. At a late stage of the refinement, atomic parameters for only the Fe4S4 cluster plus the 4 associated cystein S-gamma atoms were adjusted by least squares methods and kept fixed during the rest of the refinement. The refined model consists of 625 of the 632 nonhydrogen atoms in the protein plus 75 water molecules. Seven side chain atoms could not be located in the final electron density map. A computer program rather than visual inspection was used wherever possible in the refinement: for locating water molecules, for removing water molecules that too closely approach other atoms, for deleting atoms that lay in regions of low electron density, and for evaluating the progress of refinement. Fo-Fc Fourier refinement is sufficiently economical to be applied routinely in protein crystal structure determinations. The complete HiPIP refinement required approximately 12 hours of CDC 3600 computer time and cost less than $3000 starting from a "trial structure," based upon multipe isomorphoous replacement phases, which gave an R of 43%...

Bacterial Proteins↗
PubMed2001

UV-Induced destruction of light-harvesting complexes from purple bacterium Chromatium minutissimum.

We studied UV-induced photodestruction of the native forms of bacteriochlorophyll a (Bchl a) from chromatophores and light harvesting complexes (LHC) of the sulphur photosynthetic bacterium Chromatium minutissimum. Irradiation of chromato- phores with 365-nm light (Soret band) or 280-nm light (absorption region of aromatic amino acids) led to the destruction of all long-wavelength forms of Bchl a. The quantum yields of photodestruction produced by the 280-nm light was higher than that produced by the 365-nm light. For the spectral forms of Bchl a absorbing at 850 nm and 890 nm, the difference was about one order of magnitude, and for the form absorbing at 800 nm the difference was almost two orders of magnitude. Similar UV sensitivity was observed for the Bchl a forms from isolated LHC. As a rule, the quantum yields of photodestruction induced by UV irradiation at 280 nm were about 100-1000 times higher (approximately 10(-3)-10(-4)) than that upon red light irradiation (approximately 10(-6)-10(-7)). We found that irradiation of chromatophores at 280 nm resulted in a crosslink between the core and peripheral LHC.

Bacterial Chromatophores↗
PubMedDate not supplied

[Two-photon excitation fluorescence spectrum of the light-harvesting complex LH2 from Chromatium minutissimum within 650-745 nm range is determined by two-photon absorption of bacteriochlorophyll rather than of carotenoids].

Two-photon fluorescence excitation spectra of the peripheral light-harvesting complex LH2 from the purple photosynthetic bacterium Chromatium minutissimum were examined within the expected spectral range of the optically forbidden S1 singlet state of carotenoids. LH2 preparations isolated from wild-type and carotenoid-depleted cells were used. 100-fs laser pulses in the range of 1300-1490 nm with an energy of 7-9 mW (corresponding to one-photon absorption between 650 and 745 nm) were used for two-photon fluorescence excitation. It was shown that two-photon fluorescence excitation spectra of LH2 complex from wild and carotenoid-depleted cells are very similar to each other and to the two-photon fluorescence excitation spectrum of bacteriochlorophyll a in acetone. It was concluded that direct two-photon excitation of bacteriochlorophyll a determines the fluorescence of both samples within the 650-745 nm spectral range.

Bacteriochlorophylls↗
PubMed1991

Photoproduction of hydrogen from sewage by immobilized cells of Chromatium species IA.

Immobilized cells of two Chromatium species produced hydrogen continuously for more than 160 hr in 60% and 80% sewage. One strain showing high optimum range of sulfide tolerance (up to 9 mM) produced more hydrogen in 80% sewage while the less sulfide tolerating strain (up to 6 mM) showed hydrogen photoproduction in 60% sewage. Cells were immobilized in alginate and stable hydrogen photoproduction was observed for more than one week. Appropriate strategy necessary for the treatment of sewage and similar industrial effluents for energy reclamation is discussed.

Chromatium↗
PubMed1990

Direct voltammetry of the Chromatium vinosum enzyme, sulfide:cytochrome c oxidoreductase (flavocytochrome c552).

The electrochemistry of the enzyme, sulfide:cytochrome c oxidoreductase, also known as flavocytochrome c552 from the purple sulfur bacterium, Chromatium vinosum, has been studied using several modified electrodes. Direct electron transfer between the heme of the flavocytochrome and an electrode is observed in the presence of a redox-inactive cationic species which promotes the voltammetry of the enzyme. Quasi-reversible electron transfer was achieved using the aminoglycoside, neomycin, as a promoter at either a modified gold or polished edge-plane graphite electrode. Further evidence for direct electron transfer is provided by the catalytic response of the enzyme at the electrode in the presence of substrate. Also reported is the direct spectroelectrochemistry of flavocytochrome c552 at an optically transparent thin layer gold electrode modified with Cys-Glu-Cys in the presence of neomycin.

Chromatium↗
PubMed1990

Crystallization and characterization of Chromatium vinosum cytochrome c'.

The dimeric high spin c-type cytochrome c' from Chromatium vinosum has been crystallized and the crystals characterized by x-ray diffraction. This cytochrome c' exhibits ligand-controlled dissociation from a dimer to a monomer upon binding carbon monoxide and represents an opportunity to obtain unique information concerning cooperativity in heme proteins. The C. vinosum cytochrome c' protein crystals are grown from polyethylene glycol 4000 and grow in both space group P2(1)2(1)2(1) (a = 49.2, b = 56.7, c = 98.8 A) and space group P2(1) (a = 55, b = 94, c = 50, beta = 106.1 A) depending upon the growth rate, with the P2(1)2(1)2(1) form favored at slower growth rates. The high resolution (2.0 A) atomic structure of the P2(1)2(1)2(1) form is being determined.

Carbon Monoxide↗
PubMed1990

Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum.

We have recently described the existence of two sets of genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rbu-P2 carboxylase), rbcA-rbcB and rbcL-rbcS, in the photosynthetic purple sulfur bacterium Chromatium vinosum (Viale, A.M., Kobayashi, H., and Akazawa, T. (1989) J. Bacteriol. 171, 2391-2400). These genes were cloned in plasmid vectors, and their expression was studied in Escherichia coli. Expression of rbcA-rbcB in E. coli was obtained under the control of its own promoter. On the other hand, expression of rbcL-rbcS in this host was not observed unless these genes were cloned under the control of the tac promoter. Purified rbcA-rbcB and rbcL-rbcS products from E. coli consisted of large and small subunits in equimolar ratios. They also showed very close elution profiles to Rbu-P2 carboxylase isolated from C. vinosum in size-exclusion chromatography columns, thus suggesting hexadecameric (L8S8) structures. Vmax of Rbu-P2 carboxylase were very similar for both enzymes, but the Km values for CO2 and ribulose 1,5-bisphosphate showed some differences. Immunochemical and N-terminal amino acid sequence analyses of the large and small subunits encoded by rbcA-rbcB and rbcL-rbcS also differed, especially at the level of the small subunits. The comparisons described above as well as the analysis of C. vinosum crude extracts by anion-exchange chromatography indicated that Rbu-P2 carboxylase encoded by rbcA-rbcB was the only species detected in the photosynthetic bacterium.

Amino Acid Sequence↗
PubMed1986

Complex formation and electron transfer between mitochondrial cytochrome c and flavocytochrome c552 from Chromatium vinosum.

Flavocytochrome c552 from Chromatium vinosum catalyzes the oxidation of sulfide to sulfur using a soluble c-type cytochrome as an electron acceptor. Mitochondrial cytochrome c forms a stable complex with flavocytochrome c552 and may function as an alternative electron acceptor in vitro. The recognition site for flavocytochrome c552 on equine cytochrome c has been deduced by differential chemical modification of cytochrome c in the presence and absence of flavocytochrome c552 and by kinetic analysis of the sulfide:cytochrome c oxidoreductase activity of m-trifluoromethylphenylcarbamoyl-lysine derivatives of cytochrome c. As with mitochondrial redox partners, interaction occurs around the exposed heme edge at the "front face" of cytochrome c. However, the domain recognized by flavocytochrome c552 seems to extend to the right of the heme edge, whereas the site of interaction with mitochondrial cytochrome c oxidase and reductase is more to the left. Km but not Vmax of the electron transfer reaction with mitochondrial cytochrome c increases with increasing ionic strength. The correlation of chemical modification and ionic strength dependence data indicates that the electrostatic interaction between the two hemoproteins involves fewer ionic bonds than that with other redox partners of cytochrome c.

Acetylation↗
PubMed1987

Spectroscopic and kinetic properties of an oxygen-binding heme protein from Chromatium vinosum.

Resonance Raman and electron paramagnetic resonance spectroscopy have been utilized to identify histidine as an axial heme ligand in a high spin, heme c-containing protein isolated from the photosynthetic purple sulfur bacterium Chromatium vinosum. Resonance Raman spectroscopy has also been used to characterize the CO adduct of the C. vinosum hemoprotein. Resonance Raman spectra of the heme site obtained within 10 ns of CO photolysis from the ferrous hemoprotein are virtually identical to those of the unligated protein, indicating that there is little or no rearrangement of the heme pocket in response to ligand photolysis. The equilibrium constant for CO binding to the ferrous hemeprotein was measured to be 1.7 X 10(-5) M-1 and the CO association rate constant determined to be 5.4 X 10(3) M-1 S-1. The quantum efficiency for photodissociation of the hemoprotein X CO complex was greater than or equal to 0.9.

Carbon Monoxide↗