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Biomedical subjects

R C Fuller

Publications and source records attributed to R C Fuller.

At least 37 records · Page 2Linked to original sources
PubMed1988

Pseudomonas oleovorans as a Source of Poly(beta-Hydroxyalkanoates) for Potential Applications as Biodegradable Polyesters.

Pseudomonas oleovorans was grown in homogeneous media containing n-alkanoic acids, from formate to decanoate, as the sole carbon sources. Formation of intracellular poly(beta-hydroxyalkanoates) was observed only for hexanoate and the higher n-alkanoic acids. The maximum isolated polymer yields were approximately 30% of the cellular dry weight with growth on either octanoate or nonanoate. In most cases, the major repeating unit in the polymer had the same chain length as the n-alkanoic acid used for growth, but units with two carbon atoms less or more than the acid used as a carbon source were also generally present in the polyesters formed. Indeed, copolymers containing as many as six different types of beta-hydroxyalkanoate units were formed. The weight average molecular weights of the poly(beta-hydroxyalkanoate) copolymers produced by P. oleovorans ranged from 90,000 to 370,000. In spite of the higher cell yields obtained with octanoate and nonanoate, the use of hexanoate and heptanoate yielded higher-molecular-weight polymers. These copolyesters represent an entirely new class of biodegradable thermoplastics.

Journal Article↗
PubMed1986

Oxygen regulation of development of the photosynthetic membrane system in Chloroflexus aurantiacus.

Oxygen levels which control induction of the assembly of the pigment-protein photosynthetic polypeptides in dark-grown Chloroflexus aurantiacus were determined. The induction signal by low-oxygen tension is not directly related to the respiratory competence of these photosynthetic cells. Cytochrome c554, the primary electron donor to P865+ of the reaction center, is not present in dark-grown respiratory cells but is induced in parallel with bacteriochlorophylls a and c and at similar oxygen partial pressure. The development of these components of the photosynthetic apparatus and its electron transport chain is completely independent of the presence of any detectable light or bacteriochlorophyll c or a pigments in C. aurantiacus.

Bacteria↗
PubMed1983

Primary photochemistry in the facultative green photosynthetic bacterium Chloroflexus aurantiacus.

The mechanism of primary photochemistry has been investigated in purified cytoplasmic membranes and isolated reaction centers of Chloroflexus aurantiacus. Redox titrations on the cytoplasmic membranes indicate that the midpoint redox potential of P870, the primary electron donor bacteriochlorophyll, is +362 mV. An early electron acceptor, presumably menaquinone has Em 8.1 = -50 mV, and a tightly bound photooxidizable cytochrome c554 has Em 8.1 = +245 mV. The isolated reaction center has a bacteriochlorophyll to bacteriopheophytin ratio of 0.94:1. A two-quinone acceptor system is present, and is inhibited by o-phenanthroline. Picosecond transient absorption and kinetic measurements indicate the bacteriopheophytin and bacteriochlorophyll form an earlier electron acceptor complex.

Bacteria↗
PubMed1983

Temperature dependence of growth and membrane-bound activities of Chloroflexus aurantiacus energy metabolism.

The temperature dependence of various activities related to the energy metabolism of isolated membranes and whole cells of the thermophilic bacterium Chloroflexus aurantiacus was determined after phototrophic growth at either 40, 50, or 60 degrees C. The data obtained were expressed by use of Arrhenius plots. Maximum activities were determined at about 65 degrees C for succinate 2,4-dichlorophenol-indophenol reductase as well as NADH oxidase and at about 70 degrees C for Mg-ATPase and for light-induced proton extrusion by cells. Activation energies for Mg-ATPase and light-induced proton extrusion were about 40 kJ mol-1 from 30 degrees C to about 50 degrees C and they increased significantly at higher temperatures. Essentially the same dependency was detectable with NADH oxidase, except for an increase in activation energy below 41 degrees C. All of these responses were independent of growth temperature. Succinate-2,4-dichlorophenol-indophenol reductase showed a change in activation energy around 41 degrees C only with cells grown at 60 degrees C. Differences in the responses of cells grown at different temperatures were identified on the basis of changes from sigmoidal to hyperbolic kinetics for light saturation of proton extrusion. Moreover, the thermostability of proton extrusion was maximal when assayed at the corresponding growth temperatures. In any case, thermostability was lowest at the 65 and 68 degrees C assay temperatures. Differential scanning calorimetry with membranes revealed irreversible heat uptake from about 60 to 72 degrees C. The results are discussed in light of the activation energy for the specific growth rate, which is lowest at temperatures from 40 degrees C to the optimum at 60 degrees C.

Bacteria↗
PubMed1982

Primary photochemistry in the facultatively aerobic green photosynthetic bacterium Chloroflexus aurantiacus.

Photochemical activity was examined in membrane fragments and a purified membrane preparation from Chloroflexus. Flash-induced absorption difference spectroscopy strongly suggests a primary donor (P(865)) that is more similar to the P(870) bacteriochlorophyll a dimer found in the purple photosynthetic bacteria than it is to P(840) found in the anaerobic green bacteria. Redox measurements on P(865) and an early acceptor also indicate a photochemical system characteristic of the purple bacteria. The membrane preparation contains a tightly bound type c cytochrome, c(554), that is closely coupled to the reaction center as indicated by its ability to rereduce photooxidized P(865). Chloroflexus thus appears to be distinct photochemically from other families of photosynthetic bacteria and may occupy an important role in photosynthetic evolution.

Journal Article↗
PubMed1982

Isolation and characterization of cytoplasmic membranes and chlorosomes from the green bacterium Chloroflexus aurantiacus.

A method was developed which allows the isolation and purification of cytoplasmic membranes and chlorosomes from cells of Chloroflexus aurantiacus grown under different light conditions. The dipolar ionic detergent Deriphat (0.08%) and a sodium iodide gradient centrifugation were used in isolating cytoplasmic membranes. Chlorosomes were prepared with 0.16% of the dipolar ionic detergent Miranol and purified by a sucrose gradient centrifugation. Cytoplasmic membrane fractions prepared from either high- (3,000 W m-2), medium-(200 W m-2) or low- (7 W m-2) light-grown cells had near infrared absorption bands at 866, 808, and 755 nm in a constant characteristic absorbance ratio of 6:3.8:1. In all cytoplasmic membrane preparations, the amount of bacteriochlorophyll a (Bchl a) per cytochrome, the amount of Bchl a per reaction center, and reaction center per milligram of cytoplasmic membrane protein was found to be constant. No Bchl c was present. Five respiratory enzyme activities have been measured in the cytoplasmic membrane fraction. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of denatured cytoplasmic membrane showed many bands, but a major polypeptide with an apparent molecular weight of 8,000. In contrast, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of purified chlorosomes did not contain the 8,000-molecular-weight band but revealed only three distinct protein bands with molecular weights of 15,000, 12,000, and 6,000. Isolated chlorosomes contained Bchl c and a small, yet constant, amount of Bchl a (absorbing at 790 nm) in a molar ratio of 25:1. The data indicated that the components of the photosynthetic apparatus in the cytoplasmic membrane of Chloroflexus aurantiacus remained constant and only the amount of antenna Bchl c varied with light conditions.

Bacterial Proteins↗
PubMed1981

Isolation and development of chlorosomes in the green bacterium Chloroflexus aurantiacus.

Freeze-fracture electron microscopy was used to study further the changes in chlorosome structure during the development of the photosynthetic apparatus in Chloroflexus aurantiacus J-10-fl. During development, in response to decreased light intensity or lower oxygen tension, the number of chlorosomes per cell increased. The same conditions also led to a general thickening of chlorosomes but did not affect their length or width. The thickening of the chlorosomes paralleled increases in the bacteriochlorophyll c/bacteriochlorophyll a ratio. Semiaerobic induction of the photosynthetic apparatus did not produce a synchronous assembly of chlorosomes in all cells of a given culture. Even adjacent cells of a single filament showed great variations in the rate and extent of response. Parallel appearance of (i) approximately 5-nm particles (in a lattice configuration) in the membrane attachment site, (ii) the crystalline baseplate material (with a periodicity of approximately 6 nm) adjacent to the membrane attachment site, and (iii) the chlorosome envelope layer preceded addition of longitudinally oriented, rodlike elements (diameter, congruent to 6 m) to the chlorosome core. It is estimated that each chlorosome can funnel energy into approximately 100 reaction centers. Chlorosomes could be isolated by a simple density gradient procedure only from cells grown at low light intensity. A bacteriochlorophyll a species absorbing at 790 nm was associated with isolated chlorosomes. Lithium dodecyl sulfate-polyacrylamide gel electrophoresis of chlorosomes showed only a few low-molecular-weight polypeptides (less than 15,000).

Bacteriochlorophylls↗
PubMed1981

Semiaerobic induction of bacteriochlorophyll synthesis in the green bacterium Chloroflexus aurantiacus.

Comparison of Chloroflexus aurantiacus J-10-fl cells by freeze-fracture electron microscopy showed that cell shape and dimensions did not depend on oxygen tension or light intensity during growth. The major morphological difference between cells cultured anaerobically in the light and aerobically in the dark was the absence of chlorosomes in aerobically grown cells. C. aurantiacus cells cultured aerobically in the dark began bacteriochlorophyll synthesis immediately when shifted to either phototrophic or semiaerobic conditions. Cells adapting to phototrophic conditions grew to the same density and synthesized as much bacteriochlorophyll as nonadapting phototrophic cultures grown at the same light intensity. Cells adapting to reduced oxygen tension (semiaerobic conditions) in the dark entered an 8- to 12-h growth lag during which the bacteriochlorophyll content increased significantly. Despite variations in the initial bacteriochlorophyll content and in the length of the growth lag, the amounts of bacteriochlorophyll a and c were constant at the end of the semiaerobic growth lag. At later times during adaptation to semiaerobic conditions, after growth resumed, variations in the ratio of bacteriochlorophyll c/bacteriochlorophyll a were observed and suggested independent regulation of the two bacteriochlorophylls.

Aerobiosis↗
PubMed1977

Pigment analysis in the identification of "Flavobacteria".

Spectral properties of the intracellular pigments of flavpbacteroa were studied by "scanning" ultrasonic preparations, methanol extracts, MF preparations, slide cultures and whole cell suspensions. No genus-specific Amax were demonstrated with methanol extracts. In situ analyses of pigment, using ultrasonic preparations or whole cell suspensions, demonstrated that all strains of Flavobacterium spp. surveyed showed a discrete Amax between 418 and 421 nm. This peak was absent from scans of other yellow gram negative rods". Amplitude of Amax was accentuated by variation in incubation parameters. Good resolution was obtained by repositioning cuvettes in "conventional" spectrophotometers and attaching opal glass plates to the "detector suface" of cuvettes. The presence of a genus-specific Flavobacterium pigment, or pigment fraction, detected through in situ analysis, adds another feature to keys or schema used for characterization and identification of the organisms comprising this presently ill-defined taxon.

Carotenoids↗
PubMed1972

Protein synthesis by isolated etioplasts and chloroplasts from pea and wheat and the effects of chloramphenicol and cycloheximide.

Etioplasts capable of incorporating (14)C-leucine into protein have been isolated from dark-grown pea and wheat plants. The requirements for leucine incorporation for etioplasts were similar to those for chloroplasts. An ATP-generating system, Mg(2+), and GTP were required. The amino-acid-incorporation activity of etioplasts from wheat was comparable to that of chloroplasts on an RNA basis, whereas the activity of pea etioplasts was about 50% of the activity of pea chloroplasts. The incorporation of leucine into protein by etioplasts and chloroplasts from pea and wheat was inhibited by chloramphenicol, and to a slight extent by cycloheximide.

Journal Article↗
PubMed1972

Light-stimulated Production of a Chloroplast-localized System for Protein Synthesis in Euglena gracilis.

Chloroplasts and proplastids isolated respectively from autotrophic and dark-adapted cells of Euglena gracilis strain Z incorporated (14)C-l-leucine into protein. In each case the incorporation was inhibited by chloramphenicol (50% inhibition at about 5 mug/ml for chloroplasts and 30 mug/ml for proplastids), but not appreciably by cycloheximide at concentrations up to 200 mug/ml. Chloroplasts from autotrophic cells incorporated leucine into protein at rates of about 10 pg leucine per mg RNA in one minute, but isolated proplastids were only 5 to 10% as active. When dark-adapted cells were illuminated there was little increase in the activity of the chloroplast fraction during the first 12 hr. Between 12 and 24 hr, when there was a rapid increase in the rate of synthesis of chlorophyll, the capacity of the chloroplast fraction for protein synthesis increased markedly. Suppression of the formation of a chloroplast-localized system for protein synthesis by treating the cells with chloramphenicol and the lack of such an effect with cycloheximide suggests that certain of the proteins which form part of a functional chloroplast system for protein synthesis are themselves synthesized within the chloroplasts.

Journal Article↗
PubMed1971

The isolation and characterization of a photochemically active complex from Chloropseudomonas ethylica.

A photochemically active subcellular fraction has been isolated from the green bacterium Chloropseudomonas ethylica. It is enriched in bacteriochlorophyll a and contains only a small amount of Chlorobium chlorophyll. Both a reaction-center bleaching (P840) and a cytochrome oxidation (C553) are observed to occur in the fraction. Particles that are contained in the fraction are larger than 1.5 x 10(6) daltons and exhibit a range of sizes consistent with some form of polymeric association of similar subunits. Around 80 bacteriochlorophyll a molecules are present per P840. In an intact photosynthetic apparatus there are about 1000-1500 total chlorophylls (including Chlorobium chlorophyll) per reaction center. The redox potentials of the reaction center P840 and C553 were found to be 0.24 and 0.17 V, respectively, in one-electron reactions. The potentials of these components are around 0.2 V lower than comparable components found in other photosynthetic organisms.

Bacteria↗