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  • 1
    Keywords: Forschungsbericht ; Nanostrukturiertes Material ; Umwelttoxikologie ; Toxikologische Bewertung
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (12 Seiten, 1,29 MB) , Illustrationen
    Language: German
    Note: Förderkennzeichen BMBF 03X0150F. - Verbund-Nummer 01155640 , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden
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  • 2
    ISSN: 1432-2048
    Keywords: Chlororespiration ; Cytochrome c 553 ; Electrochromism ; Photosynthesis ; Plastocyanin ; Pleurochloris
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract For characterisation of chlororespiration in the chlorophyll c-containing alga Pleurochloris meiringensis, we measured the flash-induced electrochromic absorbance changes between 470 and 545 nm and the redox changes of cytochrome f and cytochrome c 553. Cytochrome c 553 was shown to be present in high amounts (1 mol cytochrome c 553 per 300 mol chlorophyll) in this alga and to function as the obligate electron donor for photosystem I instead of plastocyanin. Whereas salicylhydroxamic acid had no effect on the flash-induced absorbance transients, cyanide enhanced the slow-rising (t1/2≈10 ms) kinetic component of the electrochromic absorbance change. Cyanide also accelerated the re-reduction of the cytochrome f +/c 553 + electron pool following the photooxidation by repetitive single-turnover flashes. These data suggest that an oxidase competes with the cytochromes for electrons. The KCN concentration needed to induce these effects was 0.25 mM at half-saturation, whereas mitochondrial respiration was completely blocked at 0.1 mM. Therefore, the oxidase cannot be identical to the cytochrome aa3-oxidase of mitochondria and is most likely located in the chloroplast of P. meiringensis.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5176
    Keywords: fluorescence ; bioassay ; PSII herbicides ; algae ; triazines ; phenylureas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Triazines and derivatives of phenylurea, which are often found in outdoor water samples, induce specific changes in the yield of thein-vivo chlorophyll α-fluorescence of PSII. These changes are correlated quantitatively with the concentration of the herbicides and can therefore be used to set-up a low-price monitor system. In order to detect selectively the herbicide-sensitive part of the fluorescence emission a pulse amplitude modulated fluorimeter was used. The bioassay system was optimised with respect to test organism, growing and measuring conditions. The relationship between fluorescence yield and herbicide concentrations were experimentally determined for the triazines atrazine and simazine and the phenylurea herbicide DCMU and mathematically fitted (r=0.99). The I50-values were 0.9 µM for DCMU, 2.2 µM for simazine and 3.3 µM for atrazine. The detection limit of about 0.5 µM clearly shows that the sensitivity of this bioassay system is too low to reach the requirements of the drinking water regulation. However, due to its insensitivity against complex water matrices, there is good hope to combine this fluorometric bioassay with a potent herbicide preconcentration method like a solid-phase extraction procedure.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 43 (1995), S. 49-56 
    ISSN: 1573-5079
    Keywords: Xanthophyceae ; Chl-c-containing algae ; carotenoids ; electrochromic absorbance changes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Flash-induced absorbance changes were measured in the Chl-c-containing alga Pleurochloris meiringensis (Xanthophyceae) between 430 and 570 nm. In addition to the bands originating from redox changes of cytochromes, three major positive and tow negative transient bands were observed both 0.7 and 20 ms after the exciting flash. These transient bands peaking at 520, 480 and 451 nm and 497 and 465 nm, respectively, could be assigned to an almost homogeneous shift of the absorbance bands with maxima at 506, 473 and 444 nm, respectively. The shape of the absorbance transients elicited from PS I or PS II was identical, and the two photosystems contributed nearly equally to the absorbance changes. Furthermore, the decay transients were sensitive to the preillumination of the cells. These data strongly suggest that the absorbance transients originate from an electrochromic response of carotenoid molecules. The pigment species responsible for the 506 nm absorption band, probably heteroxanthin or diatoxanthin, transferred excitation energy to both photosystems as shown by the aid of 77 K fluorescence excitation spectra.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-5079
    Keywords: algae ; chlororespiration ; NAD(P)H: plastoquinone oxidoreductase ; photosynthesis ; chloroplasts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using isolated chloroplasts or purified thylakoids from photoautotrophically grown cells of the chromophytic alga Pleurochloris meiringensis (Xanthophyceae) we were able to demonstrate a membrane bound NAD(P)H dehydrogenase activity. NAD(P)H oxidation was detectable with menadione, coenzyme Q0, decylplastoquinone and decylubiquinone as acceptors in an in vitro assay. K m-values for both pyridine nucleotides were in the μmolar range (K m[NADH]=9.8 μM, K m[NADPH]=3.2 μM calculated according to Lineweaver-Burk). NADH oxidation was optimal at pH 9 while pH dependence of NADPH oxidation showed a main peak at 9.8 and a smaller optimum at pH 7.5–8. NADH oxidation could be completely inhibited with rotenone, an inhibitor of mitochondrial complex I dehydrogenase, while NADPH oxidation revealed the typical inhibition pattern upon addition of oxidized pyridine nucleotides reported for ferredoxin: NADP+ reductase. Partly-denaturing gel electrophoresis followed by NAD(P)H dehydrogenase activity staining showed that NADPH and NADH oxidizing proteins had different electrophoretic mobilities. As revealed by denaturing electrophoresis, the NADH oxidizing enzyme had one main subunit of 22 kDa and two further polypeptides of 29 and 44 kDa, whereas separation of the NADPH depending protein yielded five bands of different molecular weight. Measurement of oxygen consumption due to PS I mediated methylviologen reduction upon complete inhibition of PS II showed that the NAD(P)H dehydrogenase is able to catalyze an input of electrons from NADH to the photosynthetic electron transport chain in case of an oxidized plastoquinone-pool. We suggest ferredoxin: NADP+ reductase to be the main NADPH oxidizing activity while a thylakoidal NAD(P)H: plastoquinone oxidoreductase involved in the chlororespiratory pathway in the dark acts mainly as an NADH oxidizing enzyme.
    Type of Medium: Electronic Resource
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