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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Based on polyacrylamide/agarose gel electrophoresis (1) or sucrose gradient centrifugation (2), two methods are described for the purification of the pigmented components from the photosynthetic membranes of the bacterium Chromatium purpuratum. All fractions were characterized by SDS-polyacrylamide gel electrophoresis, electron microscopy and absorption spectroscopy. Method 2 gave pure core (the reaction center- light-harvesting pigment-protein complex 1) particles that had absorption maximum at 870 nm. Under electron microscopy they appeared as circles of 12–15 nm in diameter with protein density in the central (5–6 nm) and peripheral areas (9–15 nm), and as a trapezium of 4.5–5 nm in height with two layers of protein density and 10–12 nm and 13–15 nm bases. A model of photoreceptor units from C. purpuratum is suggested and discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 49 (1998), S. 397-425 
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract The cytochromes that function in photosynthesis in cyanobacteria, algae, and higher plants have, like the other photosynthetic catalysts, been largely conserved in their structure and function during evolution. Cyanobacteria and algae contain cytochrome c6, which is not found in higher plants and which may enhance survival in their planktonic mode of life. Cyanobacteria and algae contain another cytochrome, low-potential c549, which is not found in higher plants. This cytochrome has a structural role in PSII and may contribute to anaerobic survival. There is a third unique cytochrome, cytochrome M, in the planktonic photosynthesizers, and its function is unknown. New evidence is appearing to indicate evolution of cytochrome interaction mechanisms during the evolution of photosynthesis. The ease of cytochrome gene manipulation in cyanobacteria and in Chlamydomonas reinhardtii now provides great advantages in understanding of photosynthesis. The solution of tertiary and quaternary structures of cytochromes and cytochrome complexes will provide structural and functional detail at atomic resolution.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 54 (1997), S. 81-98 
    ISSN: 1573-5079
    Keywords: cytochrome b6f complex ; cytochrome bc1complex ; electron transfer ; Photosystem I ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract This review compares the three-dimensional structures of the solublec-type cytochromes that functionally link membrane-bound energy transducingcomplexes in algal, cyanobacterial and eubacterial photosynthesis. Inanoxygenic photosynthesis, cytochrome c2transfers electronsbetween the cytochrome bc1complex and the eubacterialreaction center. Cytochrome c6performs the analogous functionin oxygenic photosynthesis, carrying electrons between the cytochromeb6f complex and Photosystem I. One of the most strikingobservations from recent progress in elucidating the structures of themembrane-bound electron transfer partners of cytochrome c2andcytochrome c6is the structural similarity between PhotosystemI and the bacterial reaction center. Are there similarities in thestructures of cytochrome c2and cytochrome c6that are functionally relevant in the context of their interaction withtheir membrane-bound redox partners? In addition to providing a generaldescription of the structures of cytochrome c2and cytochromec6, the following comparison addresses this question.
    Type of Medium: Electronic Resource
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