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'Photosystem II' in keywords Facet   Publication Year 1988  [X]
Facet   section ZfN Section C  [X]
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1988[X]
1Author    Éva Hideg, Sándor DemeterRequires cookie*
 Title    Thermoluminescence and Delayed Luminescence Characterization of Photosystem II a and Photosystem II p Reaction Centers  
 Abstract    The thermoluminescence and delayed luminescence characteristics of PS II" and PS IIp centers were investigated in BBY particles and stroma thylakoids, respectively. The BBY particles exhib-ited a thermoluminescence band at 25 °C (B band) which was associated with the charge recombi-nation of the S 2 Qb" redox couple and underwent period-2 oscillation in a sequence of flashes. In the flash-induced decay of delayed luminescence of BBY particles a component with a half-time of 34 s corresponded to the B thermoluminescence band and was also assigned to S2OB charge recombination. No corresponding thermoluminescence or delayed luminescence components as-sociated with the secondary acceptor OB could be observed in the glow curve or delayed lumines-cence decay of stroma thylakoids. These observations indicate that unlike PS IIa the PS Hp centers are not associated with the two-electron gate, 0B. 
  Reference    Z. Naturforsch. 43c, 596—600 (1988); received May 2 1988 
  Published    1988 
  Keywords    Photosynthesis, Photosystem II, Thermoluminescence, Delayed Luminescence 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0596.pdf 
 Identifier    ZNC-1988-43c-0596 
 Volume    43 
2Author    SeymourSteven BrodyRequires cookie*
 Title    Rebinding of the 33 kDalton Polypeptide of Photosystem II to the D-l/D-2 Sub-Core Complex  
 Abstract    Specific and stoichiometric binding is shown between the D-l/D-2 sub-core complex and the 33 kDa polypeptide of photosystem II. Fluorescence from chlorophyll is used as an endogenous probe. When binding occurs there is an increase in fluorescence yield, as well as changes in both the fluorescence spectrum and excitation spectrum. 
  Reference    Z. Naturforsch. 43c, 727—730 (1988); received January 28/May 31 1988 
  Published    1988 
  Keywords    Photosynthesis, Reaction Center, Photosystem II, Chlorophyll, Fluorescence 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0727.pdf 
 Identifier    ZNC-1988-43c-0727 
 Volume    43 
3Author    Imre Vass, Narendranath Mohanty, Sándor DemeterRequires cookie*
 Title    Photoinhibition of Electron Transport Activity of Photosystem II in Isolated Thylakoids Studied by Thermoluminescence and Delayed Luminescence  
 Abstract    The effect of photoinhibition on the primary (Oa) and secondary (Ob) quinone acceptors of photosystem II was investigated in isolated spinach thylakoids by the methods of thermolumines-cence and delayed luminescence. The amplitudes of the Q (at about 2 °C) and B (at about 30 °C) thermoluminescence bands which are associated with the recombination of the S;OA and S2QB charge pairs, respectively, exhibited parallel decay courses during photoinhibitory treatment. Similarly, the amplitudes of the flash-induced delayed luminescence components ascribed to the recombination of S 2 0A and S 2 OB charge pairs and having half life-times of about 3 s and 30 s, respectively, declined in parallel with the amplitudes of the corresponding Q and B thermo-luminescence bands. The course of inhibition of thermoluminescence and delayed luminescence intensity was parallel with that of the rate of oxygen evolution. The peak positions of the B and Q thermoluminescence bands as well as the half life-times of the corresponding delayed lumines-cence components were not affected by photoinhibition. These results indicate that in isolated thylakoids neither the amount nor the stability of the reduced OB acceptor is preferentially decreased by photoinhibition. We conclude that either the primary target of photodamage is located before the Ob binding site in the reaction center of photosystem II or QA and OB undergo simultaneous damage. 
  Reference    Z. Naturforsch. 43c, 871—876 (1988); received August 12 1988 
  Published    1988 
  Keywords    Photosynthesis, Photoinhibition, Photosystem II, Thermoluminescence, Delayed Luminescence 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0871.pdf 
 Identifier    ZNC-1988-43c-0871 
 Volume    43 
4Author    Gudrun Wälzlein, AchimE. Gau, ElfriedeK. PistoriusRequires cookie*
 Title    Further Investigations about the Flavin in the L-Amino Acid Oxidase and a Possible Flavin in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    The absorption spectrum of the previously purified L-amino acid oxidase from the cyanobac-terium Anacystis nidulans has shown considerable variation with each preparation and the spec-trum in several preparations was quite different from the absorption spectrum of other simple flavoproteins (E. K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986). Here we show that the spectral complexity and variability of the L-amino acid oxidase can be largely explained by the presence of a modified flavin derivative of yet unknown structure besides oxidized FAD and FAD semiquinone. After removal from the enzyme this modified chromophore has absorption maxima at 260, 396 and in the 600 nm region. This derivative of FAD seems to be formed in variable amounts during the purification of the enzyme. On the other hand, extraction of Anacystis photosystem II complexes which contain the flavoprotein, almost exclusively yields modified flavin derivatives and practically no authentic oxidized FAD. The spectrum of the chromophores which have been extracted from photosystem II complexes at different purification stages, is either similar (although not identical) to the spectrum of the chromophore extracted from the isolated L-amino acid oxidase or similar to the spectrum of reduced flavin. All extracted chromophores show a fluorescence emission in the 420 to 560 nm region when excited with light of 390 nm. These results indicate that the flavin present in the L-amino acid oxidase protein as well as in photosystem II complexes from A. nidulans rapidly undergoes modification reactions of yet unknown nature to yield several closely related FAD derivatives. This might possibly be the reason why so far no flavin has been detected in photosys-tem II. The presence of such modified flavin derivatives in photosystem II complexes of A. nidulans as shown here is an additional support of our hypothesis that an unusual flavin is functional on the donor side of photosystem II. 
  Reference    Z. Naturforsch. 43c, 545—553 (1988); received January 25 1988 
  Published    1988 
  Keywords    L-Amino Acid Oxidase, Flavoprotein, Photosystem II, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0545.pdf 
 Identifier    ZNC-1988-43c-0545 
 Volume    43