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  • 1
    Online Resource
    Online Resource
    Dordrecht :Springer Netherlands,
    Keywords: Cyanobacteria. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (249 pages)
    Edition: 1st ed.
    ISBN: 9781402030222
    Series Statement: Aquatic Ecology Series ; v.3
    DDC: 579.3/9165
    Language: English
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  • 2
    ISSN: 1573-5079
    Keywords: cell membrane ; fluorescent energy transduction probe ; photosynthesis ; Plectonema boryanum ; respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fluorescent probe 9-amino-6-chloro-2-methoxy acridine was used to study the energy transduction in the thylakoid and cell membranes of the cyanobacterium Plectonema boryanum. Apart from light-driven electron transfer, the dark endogenous respiration also leads to energization resulting in an ACMA fluorescence response, that is sensitive to the electron flow inhibitor 2, 5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, to the energy transfer inhibitors dicyclohexylcarbodiimide and venturicidine and to the uncoupler 5-chloro-3-t-butyl-2′-chloro-4′-nitrosalicylanilide. In spheroplasts, in which the cell membranes have lost their capacity to maintain a proton gradient, the respiration-and light-induced ACMA fluorescence changes (quenching) are similar to those in chloroplasts. In intact cells a combination of reversible quenching and enhancement of ACMA fluorescence was found. This dualistic behaviour is supposedly caused by an opposite orientation of the thylakoid and cell membranes. ACMA quenching at the level of the thylakoids was obtained either by respiratory or photosynthetic electron transfer and gave similar responses to those obtained in the spheroplasts. The slower ACMA fluorescence enhancement, only observed in cells with intact cell membranes, also evoked by both respiration and light-induced energization is sensitive to the compounds mentioned above and in addition to KCN. Our results support the view [8] that dark oxidation of substrates by O2 proceeds via the thylakoid membrane and terminates at a CN- sensitive oxidase located in the cell membrane which requires the involvement of a mobile cytoplasmic redox mediator.
    Type of Medium: Electronic Resource
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