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1Author    Georg SchmettererRequires cookie*
 Title    Formation of Hydrocarbons by Photobleaching Cyanobacterium, A nacystis nidulans  
 Abstract    The cyanobacterium Anacystis nidulans is bleached when subjected to both light and 0 2 to­ gether with suitable (pre)treatment o f the cells such as incubation at high (^ 4 8 °C) or low (S 17 °C) temperatures, or in presence o f metabolic inhibitors, or o f substances forming com­ plexes with divalent cations. Concomitantly degradation o f the intracellular membranes is ob­ served (G. Schmetterer, G. A. Peschek, Biochem. Physiol. Pflanzen 176, 9 0 —100 (1981)). The same three conditions cause formation o f hydrocarbons, mostly ethane, a characteristic product of lipid peroxidation. Ethane production is unchanged and still light-sensitive even when no more pigments can be detected in the cells. In "white" cells light-dependent 0 2-uptake is also observed. The action spectrum of this process suggests that "completely" bleached cells retain very small amounts of residual chlorophyll, which must be unusually resistant to photooxidation. 
  Reference    Z. Naturforsch. 37c, 205 (1982); received November 51981 
  Published    1982 
  Keywords    Photooxidation, Ethane Production, Cyanobacterium, Anacystis nidulans, Lipid Peroxidation 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0205.pdf 
 Identifier    ZNC-1982-37c-0205 
 Volume    37 
2Author    Wilhelm Simonis, Johanna Lee-KadenRequires cookie*
 Title    Selektive  
 Abstract    Wirkungen von Lindan (y-l,2,3,4,5,6-Hexachlor-cyclohexan) auf Photosynthese, Aminosäure — Membrantransport und Proteinsynthese bei Anacystis nidulans Selective Effects of Lindane (7-1,2,3,4,5,6 Hexachlorocyclohexane) on Photosynthesis, M embrane Transport of Amino Acids and Protein Synthesis in Anacystis nidulans Effects of the chlorinated hydrocarbon insecticide Lindane on membrane transport of two neu­ trale amino acids in the Cyanobacterium Anacystis nidulans (Synechococcus AN) were measured. In white light the L-Leucine incorporation into the protein fraction was inhibited, increasing with time. After 30 minutes the degree of inhibition was the same as the effect of DCMU (5X 10-6 m) on L-Leucine incorporation. 14C 02-fixation was also reduced at this time. At 717 nm, which en­ ables PS I activity allone, no inhibition was observed. The light energy dependent membrane transport itself of L-leucine in presence of CAM and of the non-metabolisable a-AIB in white light and in monochromatic light of 630 nm and of 717 nm were not influenced by Lindane. The different sites of Lindane action are discussed. It is assumed that in 30 minutes chiefly photo­ synthesis (PS II and C 02-fixation) is affected by Lindane, resulting in a suppression of protein synthesis caused by a depletion of intermediates of C 02-fixation. 
  Reference    Z. Naturforsch. 34c, 1062—1065 (1979); eingegangen am 12. Juni 1979 
  Published    1979 
  Keywords    Anacystis nidulans, Lindane Effects, Amino Acids, Membrane Transport, Photosynthesis 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1062.pdf 
 Identifier    ZNC-1979-34c-1062 
 Volume    34 
3Author    ElfriedeK. PistoriusRequires cookie*
 Title    Further Evidence for a Functional Relationship between L-Amino Acid Oxidase Activity and Photosynthetic Oxygen Evolution in Anacystis nidulans. Effect of Chloride on the Two Reactions  
 Abstract    The L-amino acid oxidase from Anacystis nidulans is inhibited by cations as well as anions. The inhibition by cations has been previously described (E. K. Pistorius, Eur. J. Biochem. 135, 217—222 [1983]). We have shown that the order of effectiveness was > M2+ > M +, when e.g. La3+, Ca2+ and K+ were compared. However, in the concentration range where the monovalent cations inhibited, the inhibition was not entirely due to the cation, but an influence of the anion could also be observed. When monovalent anions were compared as the corresponding sodium salts, the order of effectiveness was SCN~ > N 0 3_ > CL, Br > I~ > F ' > H CO O " > CH,COO . The inhibition of the L-amino acid oxidase activity by the various salts was strongly influenced by the pH of the reaction mixture. It could be shown that the inhibition by cations increased in the alkaline pH region, while the inhibition by anions increased in the acidic pH region. Our previous results have also shown that a functional relationship might exist between L-amino acid oxidase activity and photosynthetic 0 2 evolution (E. K. Pistorius and H. Voss, Eur. J. Biochem. 126, 203—209 [1982]). Since the water-splitting complex of photosystem II is affected by a number of anions, although only Cl-and Br" lead to activation of 0 2 evolution, we investigated whether a correlation could be obtained between the anion effect on the L-amino acid oxidase and on photosynthetic 0 2 evolution. The results show that those anions which have a higher affinity for the enzyme than CL or Br", are especially effective in causing inactivation of the 0 2 evolu­ tion. Moreover, we show that L-arginine which is a substrate of the L-amino acid oxidase, and Cl-have antagonistic effects on the L-amino acid oxidase reaction and on photosynthetic 0 2 evolu­ tion. We suggest that this flavoprotein with L-amino acid oxidase activity is modified by Ca:+ and CL in such a way that it can now interact with Mn2* and catalyze the water-splitting reaction of photosystem II. 
  Reference    Z. Naturforsch. 40c, 806—813 (1985); received June 7 1985 
  Published    1985 
  Keywords    Anacystis nidulans, 0 2 Evolution, L-Amino Acid Oxidase, Chloride 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0806.pdf 
 Identifier    ZNC-1985-40c-0806 
 Volume    40 
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 
5Author    AchimE. Gau, Gudrun Wälzlein, Susanne Gärtner, Matthias Kuhlmann, Susanne Specht, ElfriedeK. PistoriusRequires cookie*
 Title    Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    Photosystem II complexes from the cyanobacterium Anacystis nidulans have been investigated by Western blots with antisera raised against four photosystem II peptides from plants and with an antiserum raised against the soluble L-amino acid oxidase protein from/1. nidulans to achieve an iden­ tification of the polypeptides — especially of the L-amino acid oxidase related protein — in isolated photosystem II complexes. Anacystis photosystem II complexes which were solubilized with lauryldimethylamine N-oxide and purified by sucrose cushion and sucrose gradient centrifugation, contained as major Coomassie brilliant blue stained polypeptides a 71 kDa band of unknown identity, a 62 kDa band, which partly contained D-l, a 55 and 49 kDa band which were immuno-reactive with an antiserum to the 47 kDa peptide of tobacco PS II complexes, and three distinct bands in the 30 kDa region. These latter bands could be identified as the extrinsic Mn stabilizing peptide (27—30 kDa), D-l (30—33 kDa) and a 36 kDa peptide (35 — 38 kDa) which crossreacted with the antiserum raised against the soluble L-amino acid oxidase protein of 50 kDa. These results suggest that the 36 kDa peptide present in purified photosystem II complexes from A. nidulans might be a processed form of the soluble 50 kDa L-amino acid oxidase protein. 
  Reference    Z. Naturforsch. 44c, 971—975 (1989); received June 22 1989 
  Published    1989 
  Keywords    Photosystem II, L-Amino Acid Oxidase, Antibody, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0971.pdf 
 Identifier    ZNC-1989-44c-0971 
 Volume    44 
6Author    ShigetohM. Iyachi11, JoachimB. Ürger, K. Iriakos, K. Otzabasisb, JensT. Hielm Annc, H. O. Rst SengerRequires cookie*
 Title    Photosynthetic Characteristics of Three Strains of Cyanobacteria Grown under Low-or High-C02 Conditions  
 Abstract    Quantum requirements of photosynthetic oxygen evolution at 679 nm, fluorescence em is­ sion spectra at liquid nitrogen temperature (77 K) and fluorescence induction kinetics in the presence of DCM U, were measured in the cyanobacteria Anabaena variabilis M3, Anabaena variabilis ATCC 29413 and A nacystis nidulans R2, each grown under low-or high-C02 condi­ tions. L o w -C 0 2 grown cells o f the cyanobacteria showed a higher quantum requirement of photosynthetic oxygen evolution and a higher ratio o f F7U)_740 to F680_700 fluorescence and a lower variable fluorescence in the presence of D CM U than high-C02 grown cells. These findings indicate a change in excitation energy distribution in favour of photosystem I. The result might be an enhancement in ATP formation caused by cyclic electron flow which in turn provokes dissolved inorganic carbon (D IC) accumulation in these low-C02 grown cells. 
  Reference    Z. Naturforsch. 51c, 40—4 (1996); received August 4/October 6 1995 
  Published    1996 
  Keywords    Quantum Requirement, Fluorescence, Dissolved Inorganic Carbon, Anabaena variabilis, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0040.pdf 
 Identifier    ZNC-1996-51c-0040 
 Volume    51 
7Author    W. LöffelhardtRequires cookie*
 Title    The Biosynthesis of Phenylacetic Acids in the Blue-Green Alga Anacystis nidulans: Evidence for the Involvement of a Thylakoid-Bound L-Amino Acid Oxidase  
 Abstract    Phenylacetic acid and p-hydroxyphenylacetic acid are formed upon incubation of photosynthetic membranes from the prokaryotic alga Anacystis nidulans with L-phenylalanine and L-tyrosine, respectively. The corresponding phenylpyruvic acids act as intermediates as shown by trapping them as the stable oximino acids. The first step in this reaction sequence appears to be catalyzed by a thylakoid-bound L-amino acid oxidase. Already existing evidence concerning phenylacetic acid formation at thylakoid membranes of higher plants via an L-amino acid oxidase and the results obtained with A. nidulans give another example of aromatic amino acids between chloroplasts and 
  Reference    (Z. Naturforsch. 32c, 345—350 [1977]; received February 14 1977) 
  Published    1977 
  Keywords    Membrane-Bound Enzymes, Anacystis nidulans, Thylakoids, Phenylacetic Acids, L-Amino Acid Oxidase 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0345.pdf 
 Identifier    ZNC-1977-32c-0345 
 Volume    32