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  • Polymer and Materials Science  (152)
  • Life Sciences  (6)
  • photosynthesis  (6)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 9 (1965), S. 2811-2817 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: When hexaphenylcyclotrisilazane was heated above 450°C. at atmospheric pressure, it formed an infusible polymer of exceptional thermal and chemical stability. The polymerization, which was accompanied by elimination of benzene, is represented approximately by the equation: \documentclass{article}\pagestyle{empty}\begin{document}$\eta [({\rm C}_6 {\rm H}_5)_2 {\rm SiNH}]_3\,\, \to \,\,({\rm C}_6 {\rm H}_5 {\rm SiN})_{3n} + 3n{\rm C}_6 {\rm H}_6$\end{document} The infusible polymer was a foamed, vitreous, pale yellow solid with a high degree of stability to heat, acids, alkali, and organic solvents. A similar reaction occured with a resein that was obtained as a by-product in the preparation of hexaphenylcyclotrisilazane and with a mixture of silylamines that was obtained from the reaction of methylphenyldichlorosilane with ammonia. Coatings on aluminum and steel prepared by heating the silylamine polymers had good thermal stability and adhesion. Inclusion of a polymeric dimethylsilyl derivative of ethylenediamine improved the flexibility of the coatings.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5079
    Keywords: cytochrome c ; photosynthesis ; photosynthetic bacteria ; electron transport ; Chloroflexus aurantiacus ; green bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The membrane-bound photooxidizable cytochrome c-554 from Chloroflexus aurantiacus has been purified. The purified protein runs as a single heme staining band on SDS-PAGE with an apparent molecular mass of 43 000 daltons. An extinction coefficient of 28 ± 1 mM−1 cm−1 per heme at 554 nm was found for the dithionite-reduced protein. The potentiometric titration of the hemes takes place over an extended range, showing clearly that the protein does not contain a single heme in a well-defined site. The titration can be fit to a Nernst curve with midpoint potentials at 0, +120, +220 and +300 mV vs the standard hydrogen electrode. Pyridine hemochrome analysis combined with a Lowry protein assay and the SDS-PAGE molecular weight indicates that there are a minimum of three, and probably four hemes per peptide. Amino acid analysis shows 5 histidine residues and 29% hydrophobic residues in the protein. This cytochrome appears to be functionally similar to the bound cytochrome from Rhodopseudomonas viridis. Both cytochrome c-554 from C. aurantiacus and the four-heme cytochrome c-558-553 from R. viridis appear to act as direct electron donors to the special bacteriochlorophyll pair of the photosynthetic reaction center. They have a similar content of hydrophobic amino acids, but differ in isoelectric point, thermodynamic characteristics, spectral properties, and in their ability to be photooxidized at low temperature.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Antonie van Leeuwenhoek 65 (1994), S. 311-329 
    ISSN: 1572-9699
    Keywords: photosynthesis ; chlorophyll ; bacteriochlorophyll ; reaction center ; electron transfer ; evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Photosynthetic reaction centers from a variety of organisms have been isolated and characterized. The groups of prokaryotic photosynthetic organisms include the purple bacteria, the filamentous green bacteria, the green sulfur bacteria and the heliobacteria as anoxygenic representatives as well as the cyanobacteria and prochlorophytes as oxygenic representatives. This review focuses on structural and functional comparisons of the various groups of photosynthetic reaction centers and considers possible evolutionary scenarios to explain the diversity of existing photosynthetic organisms.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-5079
    Keywords: photosynthesis ; Chlorobium tepidum ; antenna ; bacteriochlorophylla protein ; energy transfer ; chlorosome ; green bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The BChla-containing Fenna-Matthews-Olson (FMO) protein from the green sulfur bacteriumChlorobium tepidum was purified and characterized. Fluorescence spectra indicate that efficient excited state quenching occurs at neutral or oxidizing redox potentials. The major fluorescence lifetime at room temperature is approximately 60 ps in samples that are in neutral or oxidizing conditions, and approximately 2 ns in samples where the strong reductant sodium dithionite has been added. A similar change is observed in pump-probe picosecond absorbance difference experiments, where the long life time component increases after dithionite addition. A 16 Gauss wide EPR signal with g factor =2.005 is observed in samples without dithionite. This signal largely disappears upon addition of dithionite. Dithionite induces large reversibile changes in the 77 K absorbance spectra of the purified FMO protein and in whole cells. These results indicate that the FMO protein contains redox active groups, which may be involved in the regulation of energy transfer. Room temperature circular dichroism and low temperature absorption spectra show that dithionite also induces conformational or structural changes of the FMO protein complex.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-5079
    Keywords: photosynthesis ; bacteriochlorophyll ; electron acceptor ; iron-sulfur center ; Photosystem I ; heliobacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Treatment of membranes ofHeliobacillus mobilis with high concentrations of the chaotropic agent urea resulted in the removal of the iron-sulfur centers FA and FB from the reaction center, as indicated by EPR spectra under strongly reducing conditions. In urea-treated membranes, transient absorption measurements upon a laser flash indicated a recombination between the photo-oxidized primary donor P798+ and a reduced acceptor with a time constant of 20 ms at room temperature. Benzylviologen, vitamin K-3 and methylene blue were found to accept electrons from the reduced acceptor efficiently. A differential extinction coefficient of 225–240 mM−1 cm−1 at 798 nm was determined from experiments in the presence of methylene blue. Transient absorption difference spectra between 400 and 500 nm in the presence and absence of artificial acceptors indicated that the electron acceptor involved in the 20 ms recombination has an absorption spectrum similar to that of an iron-sulfur center. This iron-sulfur center was assigned to be analogous to FX of Photosystem I. Our results provide evidence in support of the presence of FX in heliobacteria, which was proposed on the basis of the reaction center polypeptide sequence (Liebl et al. (1993) Proc. Natl. Acad. Sci. USA 90: 7124–7128). Implications for the electron transfer pathway in the reaction center of heliobacteria are discussed.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 6 (1985), S. 317-333 
    ISSN: 1573-5079
    Keywords: bacteriochlorophyll ; cytochrome ; green bacteria ; photosynthesis ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Green bacteria make up two of the four families of anoxygenic photosynthetic prokaryotes. The two families have similar pigment compositions and membrane fine structure, and both contain a specialized antenna structure known as a chlorosome. The primary photochemistry and electron transport pathways of the two groups are, however, quite distinct. The anaerobic green bacteria (Chlorobiaceae) contain low-potential iron-sulfur proteins as early electron acceptors and can directly reduce NAD+ in a manner reminiscent of Photosystem I of oxygenic organisms. The facultatively aerobic green bacteria (Chloroflexaceae) contain quinone-type acceptors and have an overall pattern of electron transport very similar to that found in purple bacteria. Many aspects of energy storage in green bacteria, especially photophosphorylation and the role of cytochrome b/c complexes in electron transport, remain poorly understood.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-5079
    Keywords: aggregate ; antenna ; atomic force microscopy ; bacteriochlorophyllc ; chlorosome ; concentration quenching ; energy transfer ; green bacteria ; photosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The optical properties of a methyl ester homolog of bacteriochlorophylld (BChld M ) and bacteriochlorophyllc (BChlc) in H2O, hexanol-saturated H2O and methanol were studied by absorption, fluorescence emission, and circular dichroism (CD). In H2O, BChld M spontaneously forms an aggregate similar to that formed in hexane, with absorption maximum at 730 nm and fluorescence emission at 748 nm. For the pigment sample in hexanol-saturated H2O, while the absorption peaks at 661 nm, only slightly red-shifted compared to the monomer, the fluorescence emission is highly quenched. When diluted 2–3 fold with H2O, the absorption returns to around 720 nm, characteristic of an aggregate. The CD spectrum of the H2O aggregate exhibits a derivative-shaped feature with positive and negative peaks, while the amplitude is lower than that of chlorosomes. The Fourier transform infrared spectra of BChld M aggregates in H2O and hexane were measured. A 1644 cm−1 band, indicative of a bonded 131-keto group, is detected for both samples. A marker band for 5-coordinated Mg was observed at 1611 cm−1 for the two samples as well. To study the kinetic behavior of the samples, both single-photon counting (SPC) fluorescence and transient absorption difference spectroscopic measurements were performed. For BChld M in hexanol-saturated H2O, a fast decay component with a lifetime of 10 to 14 ps was detected using the two different techniques. The fast decay could be explained by the concentration quenching phenomenon due to a high local pigment concentration. For the pigment sample in H2O, SPC gave a 16 ps component, whereas global analysis of transient absorption data generated two fast components: 3.5 and 26 ps. The difference may arise from the different excitation intensities. With a much higher excitation in the latter measurements, other quenching processes, e.g. annihilation, might be introduced, giving the 3.5 ps component. Finally, atomic force microscopy was used to examine the ultrastructure of BChld M in H2O and hexanol-saturated H2O. Pigment clusters with diameters ranging from 15 to 45 nm were observed in both samples.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The polymerization of γ-benzyl-L-glutamate NCA initiated by n-hexylamine in DMF proceeds with two successive propagation rates whose ratio is about 1.5. The onset of the increase in rate of propagation occurred at a DPn of 7-14, which was independent of initiator to anhydride ratio and anhydride concentration and not a result of anhydride impurities. The increase in rate is likely a result of a conformational change in the polymer at a DPn of 7-14.
    Additional Material: 1 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 1573-1605 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The dependence of Förster long-range resonance energy transfer efficiency on the orientational freedom of donor D and acceptor A molecules attached to a macromolecular substrate is examined. The usefulness of polarized emission measurements in determining the mutual orientation as well as the degree of orientational freedom of D and A and thereby deriving maximum and minimum values for the D-A separation from the transfer efficieny is demonstrated.
    Additional Material: 20 Ill.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A thermal perturbation curve (TPC) is defined to be the derivative of the fractional degree of saturation, f, with respect to temperature, considered as a function of the natural logarithm of free ligand concentration, y. The theoretical framework for the use of such curves in the thermodynamic analysis of ligand binding to macromolecules is presented. The thermal perturbation curve either provides or complements the information obtained from the derivative binding isotherm ∂f/∂y. For a single set of identical and independent sites the TPC is identical to the derivative binding isotherm. Analysis of such a curve directly yield ΔH0 and ΔG0 for the binding reaction. In actual experimental work, however, the TPC can only be approximated because of “self-buffering” effects relations between the parameter of the approximate curve and the thermodynamic quantities have been developed. This technique is applied to the proflavin-α-chymotryspin system to demonstrate its usefulness. The general features of thermal perturbation curves for cases of multiple sets of independent sites and cooperatively interacting sites have also been developed. The analysis of thermal perturbation curves in combination with other methods should provide a more powerful approach to the characterization of ligand-macromolecule interactions.
    Additional Material: 8 Ill.
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