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  • 1
    Electronic Resource
    Electronic Resource
    Membrane-Bound c-Type Cytochromes in Heliobacillus mobilis. In Vivo Study of the Hemes Involved in Electron Donation to the Photosynthetic Reaction Center (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 11831-11839 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00037a022
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  • 2
    Electronic Resource
    Electronic Resource
    Horizontal Transfer of Genes Coding for the Photosynthetic Reaction Centers of Purple Bacteria (1997)
    Springer
    Journal of molecular evolution 45 (1997), S. 131 -136 
    Details
    ISSN: 1432-1432
    Keywords: Key words: Reaction center — Purple bacteria — Photosynthesis — Gene transfer — Evolution — Phylogenetic tree — Nucleotide sequence — Polymerase chain reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Phylogenetic trees were drawn and analyzed based on the nucleotide sequences of the 1.5-kb gene fragment coding for the L and M subunits of the photochemical reaction center of various purple photosynthetic bacteria. These trees are mostly consistent with phylogenetic trees based on 16S rRNA and soluble cytochrome c, but differ in some significant details. This inconsistency implies horizontal transfer of the genes that code for the photosynthetic apparatus in purple bacteria. Possibilities of similar transfers of photosynthesis genes during the evolution of photosynthesis are discussed especially for the establishment of oxygenic photosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006212
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  • 3
    Electronic Resource
    Electronic Resource
    Quinones in chlorosomes of green sulfur bacteria and their role in the redox-dependent fluorescence studied in chlorosome-like bacteriochlorophyll c aggregates (1997)
    Springer
    Archives of microbiology 167 (1997), S. 343-349 
    Details
    ISSN: 1432-072X
    Keywords: Key words Chlorobiumquinone ; Isoprenoid quinone ; Chlorosome ; Bacteriochlorophyll c ; Fluorescence ; Quenching ; Energy transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The light-harvesting chlorosome antennae of anaerobic, photosynthetic green sulfur bacteria exhibit a highly redox-dependent fluorescence such that the fluorescence intensity decreases under oxidizing conditions. We found that chlorosomes from Chlorobium tepidum contain three isoprenoid quinone species (chlorobiumquinone, menaquinone-7, and an unidentified quinone that probably is a chlorobiumquinone derivative) at a total concentration of approximately 0.1 mol per mol bacteriochlorophyll c. Most of the cellular chlorobiumquinone was found in the chlorosomes and constituted about 70% of the total chlorosome quinone pool. When the quinones were added to artificial, chlorosome-like bacteriochlorophyll c aggregates in an aqueous solution, a high redox dependency of the fluorescence was observed. Chlorobiumquinones were most effective in this respect. A lesser redox dependency of the fluorescence was still observed in the absence of quinones, probably due to another unidentified redox-active component. These results suggest that quinones play a significant, but not exclusive role in controlling the fluorescence and in inhibiting energy transfer in chlorosomes under oxic conditions. Chlorosomes from Chloroflexus aurantiacus contained menaquinone in an amount similar to that of total quinone in Chlorobium tepdium chlorosomes, but did not contain chlorobiumquinones. This may explain the much lower redox-dependent fluorescence observed in Chloroflexus chlorosomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050453
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  • 4
    Electronic Resource
    Electronic Resource
    Pheophytinization of bacteriochlorophyll c and energy transfer in cells of Chlorobium tepidum (1999)
    Springer
    Archives of microbiology 172 (1999), S. 40-44 
    Details
    ISSN: 1432-072X
    Keywords: Key words Bacteriochlorophyll c ; Bacteriochlorophyll a ; Bacteriopheophytin c ; Chlorobium tepidum ; Chlorosome ; Energy transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Bacteriochlorophyll (BChl) c in whole cells of Chlorobium tepidum grown at 46 °C changed into bacteriopheophytin (BPhe) c within 10 days after reaching full growth. When a small amount of C. tepidum cells in which BChl c had been completely pheophytinized were transferred to a new culture medium, normal growth was observed after a short lag phase, and the absorption spectrum of the growing cells showed the presence of a normal amount of BChl c. During the growth of C. tepidum in the new culture, the BChl c concentration was nearly proportional to the cell density measured by turbidity (OD640). These results indicate that C. tepidum can survive even when BChl c has been completely pheophytinized and that BChl c is newly synthesized in such cells when transferred to a new culture medium. In partly pheophytinized cells, upon excitation of BPhe c at 550 nm the fluorescence emission spectrum showed maxima at 775 and 810 nm, which correspond to emissions from BChl c and BChl a, respectively. This indicates energy transfer from BPhe c to BChl c and BChl a. In cells in which BChl c was completely pheophytinized, fluorescence measurements were indicative of direct energy transfer from BPhe c to baseplate BChl a. These findings suggest that when BChl c in C. tepidum cells is pheophytinized, the product (BPhe c) remains in the chlorosomes and continues to work as a light-harvesting pigment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050737
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  • 5
    Electronic Resource
    Electronic Resource
    Active and energy-dependent rapid formation of cell aggregates in the thermophilic photosynthetic bacterium Chloroflexus aggregans (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 208 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The thermophilic filamentous phototroph Chloroflexus aggregans was able to form a bacterial mat-like dense cell aggregate rapidly. The aggregate formation, which was observed in growing cells in a liquid medium in a bottle, occurred every time within 20–30 min after the cells were dispersed by shaking. The aggregation depended on the energy supplied by photosynthesis or respiration. Cells aggregated most rapidly under temperature and pH conditions that support maximum growth. The aggregation was also accelerated by the addition of 3-isobutyl-1-methylxanthine that inhibits cyclic 3′,5′-AMP phosphodiesterase. Microscopic observation revealed that the bacterium has a fast gliding mobility (1–3 μm s−1). The distinctive cell aggregation of C. aggregans was due to this rapid gliding movement.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11094.x
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  • 6
    Electronic Resource
    Electronic Resource
    Comparative and evolutionary aspects of the photosynthetic electron transfer system of purple bacteria (1994)
    Springer
    Journal of plant research 107 (1994), S. 191-200 
    Details
    ISSN: 1618-0860
    Keywords: Photosynthesis ; Electron transfer ; Purple bacteria ; Reaction center ; Cytochromec ; Cytochromebc complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cyclic electron transfer system in purple bacteria is composed of the photosynthetic reaction center, the cytochromebc 1 complex, cytochromec 2, and ubiquinone. These components share many characteristics with those of photosynthesis and respiration in other organisms. Studies of the cyclic electron transfer system have provided useful insights about the evolution and general mechanisms of membranous energy-conserving systems. The photosynthetic system in purple bacteria may represent a prototype of highly efficient, energy-conserving electron transfer systems in the organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02346017
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  • 7
    Electronic Resource
    Electronic Resource
    Dielectric behavior of copolymer and blockpolymer (methylacrylate-styrene) (1964)
    Springer
    Colloid & polymer science 200 (1964), S. 51-52 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01499439
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  • 8
    Electronic Resource
    Electronic Resource
    Comparative analysis of the primary structure of the reaction center-bound cytochrome subunit in purple bacteria (1998)
    Springer
    Photosynthesis research 55 (1998), S. 349-355 
    Details
    ISSN: 1573-5079
    Keywords: amino acid sequence ; charge interaction ; cyclic electron transfer ; cytochrome ; purple photosynthetic bacteria ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The amino acid sequences of the reaction center-bound cytochrome subunit of six species of purple bacteria were compared. Amino acid residues thought to be important in controlling the redox midpoint potentials of four hemes in Blastochloris (Rhodopseudomonas) viridis were found to be well conserved. As opposed to all other species studied, the amino acid sequence of the cytochrome subunit of B. viridis had several insertions of more than 10 residues at specific regions close to the LM core, suggesting that interaction of the cytochrome subunit with the LM core in most species is different from that in B. viridis. Distribution of charged amino acid residues on the surface of the cytochrome subunit was compared among six species and discussed from the viewpoint of interaction with soluble electron donors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005912810674
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  • 9
    Electronic Resource
    Electronic Resource
    Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum (1994)
    Springer
    Photosynthesis research 41 (1994), S. 125-134 
    Details
    ISSN: 1573-5079
    Keywords: cytochromec ; electron transfer ; green sulfur bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We studied the photosynthetic electron transfer system of membrane-bound and soluble cytochromec inChlorobium tepidum, a thermophilic green sulfur bacterium, using whole cells and membrane preparations. Sulfide and thiosulfate, physiological electron donors, enhanced flash-induced photo-oxidation ofc-type cytochromes in whole cells. In membranes,c-553 cytochromes with two (or three) heme groups served as immediate electron donors for photo-oxidized bacteriochlorophyll (P840) in the reaction center, and appeared to be closely associated with the reaction center complex. The membrane-bound cytochromec-553 had anE m-value of 180 mV. When isolated soluble cytochromec-553, which has an apparent molecular weight of 10 kDa and seems to correspond to the cytochromec-555 inChlorobium limicola andChlorobium vibrioforme, was added to a membrane suspension, rapid photo-oxidation of both soluble and membrane-bound cytochromesc-553 was observed. The oxidation of soluble cytochromec-553 was inhibited by high salt concentrations. In whole cells, photo-oxidation was observed in the absence of exogenous electron donors and re-reduction was inhibited by stigmatellin, an inhibitor of the cytochromebc complex. These results suggest that the role of membrane-bound and soluble cytochromec inC. tepidum is similar to the role of cytochromec in the photosynthetic electron transfer system of purple bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02184152
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  • 10
    Electronic Resource
    Electronic Resource
    Phylogenetic analysis of photosynthetic genes of Rhodocyclus gelatinosus: Possibility of horizontal gene transfer in purple bacteria (1993)
    Springer
    Photosynthesis research 36 (1993), S. 185-191 
    Details
    ISSN: 1573-5079
    Keywords: bound cytochrome subunit ; nucleotide sequence ; phylogeny ; reaction center ; photosynthetic bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nucleotide sequences of the genes coding for the M and cytochrome subunits of the photosynthetic reaction center of Rhodocyclus gelatinosus, a purple bacterium in the β subdivision, were determined. The deduced amino acid sequences of these proteins were compared with those of other photosynthetic bacteria. Based on the homology of these two photosynthetic proteins, Rc. gelatinosus was placed in the α subdivision of purple bacteria, which disagrees with the phylogenetic trees based on 16S rRNA and soluble cytochrome c 2. Horizontal transfer of the genes which code for the photosynthetic apparatus in purple bacteria can be postulated if the phylogenetic trees based on 16S rRNA and soluble cytochrome c 2 reflect the real history of purple bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00033037
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