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  • 1
    Electronic Resource
    Electronic Resource
    The photoproduction of superoxide radicals and the superoxide dismutase activity of Photosystem II. The possible involvement of cytochrome b559 (1994)
    Springer
    Photosynthesis research 41 (1994), S. 327-338 
    Details
    ISSN: 1573-5079
    Keywords: photosynthesis ; Photosystem II ; superoxide radical ; superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the present study the light induced formation of superoxide and intrinsic superoxide dismutase (SOD) activity in PS II membrane fragments and D1/D2/Cytb559-complexes from spinach have been analyzed by the use of ferricytochrome c (cyt c(III)) reduction and xanthine/xanthine oxidase as assay systems. The following results were obtained: 1.) Photoreduction of Cyt c (III) by PS II membrane fragments is induced by addition of sodium azide, tetracyane ethylene (TCNE) or carbonylcyanide-p-trifluoromethoxy-phenylhydrazone (FCCP) and after removal of the extrinsic polypeptides by a 1M CaCl2-treatment. This activity which is absent in control samples becomes completely inhibited by the addition of exogenous SOD. 2.) The TCNE induced cyt c(III) photoreduction by PS II membrane fragments was found to be characterized by a half maximal concentration of c1/2=10 μM TCNE. Simultaneously, TCNE inhibits the oxygen evolution rate of PS II membrane fragments with c1/2≈ 3 μM. 3.) The photoproduction of O2 − is coupled with H+-uptake. This effect is diminished by the addition of the O2 −-trap cyt c(III). 4.) D1/D2/Cytb559-complexes and PS II membrane fragments deprived of the extrinsic proteins and manganese exhibit no SOD-activity but are capable of producing O2 − in the light if a PS II electron donor is added. Based on these results the site(s) of light induced superoxide formation in PS II is (are) inferred to be located at the acceptor side. A part of the PS II donor side and Cyt b559 in its HP-form are proposed to provide an intrinsic superoxide dismutase (SOD) activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019410
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach (1987)
    Springer
    Photosynthesis research 13 (1987), S. 167-184 
    Details
    ISSN: 1573-5079
    Keywords: H+-oscillation ; photosystem II ; protolytic reactions ; Q-400(Fe2+) ; water oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The protolytic reactions of PSII membrane fragments were analyzed by measurements of absorption changes of the water soluble indicator dye bromocresol purple induced by a train of 10 μs flashes in dark-adapted samples. It was found that: a) in the first flash a rapid H+-release takes place followed by a slower H+-uptake. The deprotonation is insensitive to DCMU but is completely eliminated by linolenic acid treatment of the samples; b) the extent of the H+-uptake in the first flash depends on the redox potential of the suspension. In this time domain no H+-uptake is observed in the subsequent flashes; c) the extent of the H+-release as a function of the flash number in the sequence exhibits a characteristic oscillation pattern. Multiphasic release kinetics are observed. The oscillation pattern can be satisfactorily described by a 1, 0, 1, 2 stoichiometry for the redox transitions Si → Si+1 (i=0, 1, 2, 3) in the water oxidizing enzyme system Y. The H+-uptake after the first flash is assumed to be a consequence of the very fast reduction of oxidized Q400(Fe3+) formed due to dark incubation with K3[Fe(CN)6]. The possible participation of component Z in the deprotonation reactions at the PSII donor side is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00035239
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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