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1Author    Z. NaturforschRequires cookie*
 Title    D istribution o f Thioredoxins in Cyanobacteria  
 Abstract    The presence o f thioredoxin was demonstrated in 20 strains o f cyanobacteria as well as in one phototrophic bac­ terium Rhodopseudomonas sulfidophila and in Thiobacillus denitrificans. Thioredoxin activity was not found in Cyano-phora paradoxa and in Porphyridium cruentum using the thioredoxin-dependent PAPS-sulfotransferase activity from Synechococcus 6301 as assay system. 
  Reference    Z. Naturforsch. 34c, 1272—1274 (1979); received July 6 1979 
  Published    1979 
  Keywords    Thioredoxin, Cyanobacteria, Sulfotransferase Activation 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1272_n.pdf 
 Identifier    ZNC-1979-34c-1272_n 
 Volume    34 
2Author    A.-KJ. Sallal, N. A. NimerRequires cookie*
 Title    The Presence of Malate Dehydrogenase in Thylakoids of Anabaena cylindrical Nostoc muscorum and Chlorogloeopsis fritschii  
 Abstract    The location o f malate dehydrogenase in the cyanobacteria, Anabaena cylindrica, Nostoc muscorum and Chlorogloeopsis fritsch ii was investigated by the fractionation o f cell-free ex­ tracts. The bulk o f the enzyme activity was associated with the thylakoid membrane fraction, which also exhibited complete photosynthetic electron transport reactions. Malate dehydro­ genase activity and photosystem II activities were inhibited by hom ologous antisera raised against isolated thylakoid membranes. 
  Reference    Z. Naturforsch. 45c, 249 (1990); received July 4/O ctober 13 1989 
  Published    1990 
  Keywords    Cyanobacteria, Malate Dehydrogenase, Thylakoids 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0249.pdf 
 Identifier    ZNC-1990-45c-0249 
 Volume    45 
3Author    SeymourSteven Brody, George Papageorgiou, Katerina Alygizaki-ZorbaRequires cookie*
 Title    Photodynamic Action of Hypericin on Cyanobacteria, Synechocystis and Synechoccus (Anacystis nidulans)  
 Abstract    The photodynamic action of hypericin on photosynthesis and respiration were monitored in Synechocystis sp PCC 6803 and Synechoccus A TC C 6311 (Anacystis nidulans). An oxygen electrode was used to measure net oxygen evolution or consumption. The amount o f hyperi­ cin required to inhibit photosynthesis was quantitively determined. Photosynthesis was com­ pletely inhibited in Synechocystis when the molar ratio of chlorophyll/hypericin was about 70:1. Higher concentrations o f hypericin did not stop the uptake of oxygen, but rather stim­ ulated the process in the light. Hypericin was readily washed out o f the cells forming no permanent associations in the bacterial cell. Hypericin inhibited electron transfer and conse­ quently oxygen production by PSII particles. For half maximum inhibition o f oxygen evolu­ tion, with PSII membrane particles, the molar ratio of chlorophyll/hypericin was about 10:1. 
  Reference    Z. Naturforsch. 52c, 165—168 (1997); received November 14. 1996/January 15 1997 
  Published    1997 
  Keywords    Hypericin, Cyanobacteria, Photosynthesis, Photodynamic Action 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0165.pdf 
 Identifier    ZNC-1997-52c-0165 
 Volume    52 
4Author    Hans-Jürgen Tiburzy, RichardJ. BerzbornRequires cookie*
 Title    Subunit II (b') and Not Subunit I (b) of Photosynthetic ATP Synthases is Equivalent to Subunit b of the ATP Synthases from Nonphotosynthetic Eubacteria. Evidence for a New Assignment of b-Type F0 Subunits  
 Abstract    Subunit I of chloroplast ATP synthase is reviewed until now to be equivalent to subunit b of Escherichia coli ATP synthase, whereas subunit II is suggested to be an additional subunit in photosynthetic ATP synthases lacking a counterpart in E. coli. A fter publication of some sequences of subunits II a revision of this assignment is necessary. Based on the analysis of 51 amino acid sequences of b-type subunits concerning similarities in primary structure, iso­ electric point and a discovered discontinuous structural feature, our data provide evidence that chloroplast subunit II (subunit b' of photosynthetic eubacteria) and not chloroplast subunit I (subunit b of photosynthetic eubacteria) is the equivalent of subunit b of nonphoto­ synthetic eubacteria, and therefore does have a counterpart in e.g. E. coli. In consequence, structural features essential for function should be looked for on subunit II (b'). 
  Reference    Z. Naturforsch. 52c, 789—798 (1997); received August 1 1997 
  Published    1997 
  Keywords    Chloroplast, Coupling Factor, Stalk, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0789.pdf 
 Identifier    ZNC-1997-52c-0789 
 Volume    52 
5Author    GeoffreyA. Codd, G. Eorg, H. SchmidRequires cookie*
 Title    Effects of S-^^-DichlorophenyO-N-N'-Dimethylurea on Oxygen Evolution and Fluorescence by Whole Filaments and Isolated Thylakoids of the Cyanobacterium Anabaena cylindrica  
 Abstract    The site of inhibition of DCM U against photosystem II in the cyanobacterium (Blue-green alga) Anabaena cylindrica was examined in electron transport and fluorescence studies. Isolated thylakoids catalyzed silicomolybdate photoreduction using H zO as electron donor; the steady-state reaction was completely inhibited by DCM U. This reaction is insensitive to DCM U in chloro­ plasts, since silicomolybdate accepts electrons from the prim ary photosystem II acceptor, and thus before the site of action o f D CM U in higher plants. DCM U did not increase the steady-state level of fluorescence by inact A. cylindrica, nor affect the monophasic fluorescence induction, with 
  Reference    Z. Naturforsch. 35c, 649—655 (1980); received April 18 1980 
  Published    1980 
  Keywords    Oxygen-Evolving Side, Cyanobacteria, D CM U-Sensitivity, Fluorescence 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0649.pdf 
 Identifier    ZNC-1980-35c-0649 
 Volume    35 
6Author    PatrickC. Hallenbeck, LeonV. Kochian, JohnR. BenemannRequires cookie*
 Title    Hydrogen Evolution Catalyzed by Hydrogenase in Cultures of Cyanobacteria  
 Abstract    Cultures of Anabaena cylindrica, grown on media containing 5 m M N H 4C1 (which represses heterocyst formation), evolved hydrogen after a period o f dark incubation under an argon atmosphere. This hydrogen production was not due to nitrogenase activity, which was nearly undetectable, but was due to a hydrogenase. Cultures grown on media with tungsten substituted for molybdenum had a high frequency of heterocysts (15%) and inactive nitrogenase after nitrogen starvation. The hydrogenase activity of these cultures was three-fold greater than the activity of non-heterocystous cultures. The effects o f oxygen inhibition on hydrogen evolution by hetero-cystous cultures suggest that two pools o f hydrogenase activity exist — an oxygen sensitive hydrogen evolution in vegetative cells and a relatively oxygen-resistent hydrogen evolution in heterocysts. In either case, inhibition by oxygen was reversible. Light had an inhibitory effect on net hydrogen evolution. Hydrogen production in vitro was much higher than in vivo, indicating that in vivo hydrogenase activity is limited by endogenous reductant supply. 
  Reference    Z. Naturforsch. 36c, 87 (1981); received June 13/August 25 1980 
  Published    1981 
  Keywords    Hydrogenase, Cyanobacteria, Heterocysts, Hydrogen Evolution, Hydrogen Metabolism 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0087.pdf 
 Identifier    ZNC-1981-36c-0087 
 Volume    36 
7Author    S. Achio, M. Iyairi, N. Th, H. SchatzRequires cookie*
 Title    Oxygen-Evolving Extracts from a Thermophilic Cyanobacterium Synechococcus sp  
 Abstract    Spheroplast membranes o f a thermophilic cyanobacterium Synechococcus sp. have been treated with the detergent lauryldim ethylam ine oxide (LD A O). The resulting extracts show (1) light-induced 0 2 evolution with artificial electron acceptors, (2) four-fold enhancement o f the 0 2 evolution relative to chlorophyll, (3) parallel increase o f both the molar ratios o f PS 2/C hl and cyt b559/C hl in the extract, (4) dissociation o f the auxiliary pigm ent phycocyanin upon treatment with LDAO, but still tight association o f allophycocyanin to the photosystem 2 preparation. 
  Reference    Z. Naturforsch. 38c, 44 (1983); received July 2/Septem ber 13 1982 
  Published    1983 
  Keywords    Cyanobacteria, Oxygen Evolution, Photosystem 2, Allophycocyanin, Energy Transfer 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0044.pdf 
 Identifier    ZNC-1983-38c-0044 
 Volume    38 
8Author    Ahlert Schmidt, Elisabeth KrämerRequires cookie*
 Title    A Membrane Bound Cysteine Oxydase from the Cyanobacterium Synechococcus 6301  
 Abstract    Membrane fractions o f the cyanobacterium Synechococcus 6301 obtained by french press treatment following sonication catalyzed an oxygen-dependent oxydation o f cysteine to cystine. For 1 0 2 consumed four cysteine were oxydized. O xygen uptake was com pletely inhibited by 1 mM KCN. Only D-and L-cysteine were active and partial activity was observed with DL-homocysteine and cysteamine. N o activity was found with glutathione, mercaptoethanol, thioglycerol, dithioerythritol, or N-acetyl-L-cysteine. Cysteines with a blocked acid group such as O-methyl-L-cysteine and O-ethyl-L-cysteine were oxydized rapidly by Synechococcus m em brane fractions. Rates o f about 200 (imol o f cysteine oxydized per mg chlorophyll and hour were measured. This cysteine respiration is discussed in relation to dark inactivation o f enzymes. 
  Reference    Z. Naturforsch. 38c, 446—450 (1983); received February 22 1983 
  Published    1983 
  Keywords    Cysteine Oxydation, Oxygen, Thiol Compounds, Synechococcus, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0446.pdf 
 Identifier    ZNC-1983-38c-0446 
 Volume    38 
9Author    E. K. Pistorius, G. H. SchmidRequires cookie*
 Title    Studies on the O2 Evolution under Flash Light Illumination in Preparations of A nacystis nidulans  
 Abstract    The 0 2 yield under flash light illum ination in preparations o f Anacystis nidulans was exam ined in the presence o f redox components such as ferricyanide and ferrocyanide. W hen ferricyanide (1 mM) was added to the lyophilized, lysozym e treated and ED TA w ashed cells o f A. nidulans the familiar Joliot-Kok oscillalion with m axim um on the third flash and periodicity o f four was observed (in the presence o f added CaCl2 and M nCl2). H owever, when the ferricyanide con­ centration was increased to about 8 m M , a reduction o f the 0 2 evolution under flash illum ination was observed, and an 0 2 uptake could clearly be seen under the First and second flash. This 0 2 uptake was inhibited by D C M U and o-phenanthroline, but was not influenced by KCN or salicylhydroxamic acid. As ferrocyanide was progressively added to 1 m M ferricyanide, the oscillations faded out and the steady-state 0 2 evolution decreased. Light would progressively increase the 0 2 evolution and reduce the dam ping o f the oscillations. Two patterns o f 0 2 evolution under short saturating light flashes were observed with these Anacystis preparations on first illum ination in the presence o f cations but in the absence o f ferri­ cyanide. One pattern corresponded to the typical pattern w hich has been repeatedly described in the literature, but the second pattern gave the indication o f an initial "over-reduced" state o f the photosystem II reaction center. W ith suitable procedures the two patterns were interchangeable. Moreover, the effect o f L-arginine on the flash pattern was exam ined. The results are discussed in connection with the possible dual function o f the previously described flavin protein as an L-amino acid oxidase and as a com ponent o f the 0 2 evolving reaction center (E. K. Pistorius and H. Voss, Eur. J. Biochemistry 1 2 6 ,2 0 3 -2 0 9 (1982)). 
  Reference    Z. Naturforsch. 39c, 1097—1103 (1984); received August 20 1984 
  Published    1984 
  Keywords    0 2 Evolution, Photosystem II, Cyanobacteria, A nacystis nidulans 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1097.pdf 
 Identifier    ZNC-1984-39c-1097 
 Volume    39 
10Author    G. Wanner, G. Henkelmann, A. Schmidt, H.-P KöstRequires cookie*
 Title    Nitrogen and Sulfur Starvation of the Cyanobacterium Synechococcus 6301 An Ultrastructural, Morphometrical, and Biochemical Comparison  
 Abstract    The effects of nitrogen and sulfur limitation on various cellular parameters of the cyanobac­ terium Synechococcus 6301 were studied by electron microscopy, morphometry and biochemical methods. Nitrate and sulfate starvation for 70 h results in a massive glycogen accumulation in parallel to a loss of soluble protein and chlorophyll. Phycobilisomes disappear prior to the degra­ dation of photosynthetic membranes. For sulfate-starved cells, a formation of "storage granules" (poly-ß-hydroxy-butyric acid) is typical which amount up to 10% of the cell volume. The composi­ tion of polar lipids is simple: equal parts of C 16:0 and C 16:1 are present under all nutritional conditions; their amount is directly correlated with the total cellular membrane area as deter­ mined by morphometry. Nitrate starved cells regenerate almost completely in structure and composition within 9 h after nitrate supplementation. Regeneration of sulfate starved cells is retarded; in spite of significant synthesis of phycocyanin within 9 h the cells still exhibit marked signs of starvation. In tro d u ctio n 
  Reference    Z. Naturforsch. 41c, 741 (1986); received February 2/May 15 1986 
  Published    1986 
  Keywords    Cyanobacteria, Synechococcus Phycobiliproteins, Nitrogen Starvation, Sulfur Starvation 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0741.pdf 
 Identifier    ZNC-1986-41c-0741 
 Volume    41 
11Author    Wim Vermaas, Jeroen Charité, Gaozhong ShenRequires cookie*
 Title    Q a Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II  
 Abstract    Two D 2 mutants were created with a site-directed mutation near the presumable binding site of Q a. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to Q A and/or in binding of Q A, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photohetero-troph. In another mutant the Gly-215 residue, located next to the His residue that is pro­ posed to bind Q a and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction cen­ ters on a chlorophyll basis. We propose that proper binding of Q A to the photosystem II reac­ tion center complex is a prerequisite for stability of the photosystem II complex. Impairment of Q a binding leads to rapid inactivation of photosystem II, which may be followed by a struc­ tural disintegration of the complex. 
  Reference    Z. Naturforsch. 45c, 359—365 (1990); received November 3 1989 
  Published    1990 
  Keywords    Photoinhibition, Plastoquinone, Photosynthesis, Site-Directed Mutagenesis, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0359.pdf 
 Identifier    ZNC-1990-45c-0359 
 Volume    45 
12Author    H.E A Schenk, M. G. Bayer, T. L. Maier, A. Lüttke, U.B G Ebhart, S. StevanovicRequires cookie*
 Title    Ferredoxin-NADP+ Oxidoreductase of C. paradoxa Nucleus Encoded, but Cyanobacterial Gene Transfer from Symbiont to Host, an Evolutionary Mechanism Originating New Species  
 Abstract    The nucleus encoded cyanoplast ("cyanellar") ferredoxin-N A D P+ -oxidoreductase (F N R) o f Cyanophora paradoxa, characterized by an N-terminal amino acid sequence, is compared with hom ologous sequences o f other photoautotrophic organisms. The high degree o f similari­ ty to the cyanobacterial sequences indicates a cyanobacterial origin. This could be a first direct demonstration o f an intertaxonic combination; a gene transfer from an original endocytobiont (cyanobacterium) to the nucleus o f its host, one o f the most important demands o f the Endo-symbiosis Theory, an evolutionary mechanism leading to the origin o f a new species. 
  Reference    Z. Naturforsch. 47c, 387—3 (1992); received December 4 1991/February 10 1992 
  Published    1992 
  Keywords    C yanophoraparadoxa, G laucocystophyta, Cyanobacteria, Cyanelles, Cyanoplasts 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0387.pdf 
 Identifier    ZNC-1992-47c-0387 
 Volume    47 
13Author    I. Perewoska, C. Vernotte, M. Picaud, C. AstierRequires cookie*
 Title    Mutations in the Subunit of Photosystem II and Resistance to the Phenol Type Herbicide Ioxynil in Synechocystis PCC 6714 and 6803  
 Abstract    Several herbicides block the photosystem II electron transfer because they compete with QB, the second stable electron acceptor o f photosystem II for binding to the D, subunit. We have previously isolated a mutant o f Synechocystis 6714 in which Asn is replaced by Thr at position 266 o f D, (G. Ajlani, I. Meyer, C. Vernotte, and Astier, FEBS Lett. 246, 2 0 7 -2 1 0 (1989)) and presenting resistance to ioxynil but not to D C M U . In this report we present selection, from this mutant, o f a double mutant with an additional substitution at position 264 (Ser by Ala). The sensitivity o f this mutant toward several herbicides is given and compared to those o f the mutants having only one substitution at 266 and one substitution at 264. It was also compared to a mutant o f Chlamydomonas having the same substitutions. This allows us to discuss the interaction o f various herbicides with the D , protein and to compare the herbicide binding niches o f Chlamydomonas and Synechocystis. 
  Reference    Z. Naturforsch. 47c, 580—5 (1992); received March 13 1992 
  Published    1992 
  Keywords    Cyanobacteria, Chlamydomonas, Herbicide-Resistant M utants, Photosynthesis, Sequence Analysis 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0580.pdf 
 Identifier    ZNC-1992-47c-0580 
 Volume    47 
14Author    H. Adar Kless3, Michal Oren-Shamirb, ItzhakO. Hadc, M. Arvin Edelm, Wim VermaasaRequires cookie*
 Title    Protein Modifications in the D 2 Protein of Photosystem II Affect Properties of the Q B/Herbicide-Binding Environment  
 Abstract    The D 2 protein contains an extended loop (the D-de loop) between helices D and de at the reducing side o f photosystem II (PS II). Characterization o f D 2 mutants o f the cyanobacte­ rium Synechocystis sp. PCC 6803 has indicated that the length and amino acid com position o f the D-de loop are not critical for basic PS II functions, although most o f the residues in that region are conserved phylogenetically. Here we show using herbicide binding and electron-flow inhibition measurements that drastic modifications in the D-de loop o f the D 2 protein modify the interaction o f some PS II-directed herbicides with their binding niche. The stability o f (semi-)reduced Q B in its binding pocket is altered in at least two o f the mutants, as indicated by a shifted peak temperature o f the thermoluminescence signal originating from charge recombi­ nation involving QB. These results suggest a close functional association between the D-de loop o f the D 2 protein and the Q B/herbicide-binding environment, which is viewed as being coordinated mostly by re­ sidues o f the D 1 protein. This represents one o f the first examples o f m odification o f the Q B/ herbicide-binding domain by mutations in the D 2 protein. 
  Reference    Z. Naturforsch. 48c, 185—190 (1993); received November 23 1992 
  Published    1993 
  Keywords    Herbicides, Plastoquinone, Photosystem II, Thermoluminescence, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0185.pdf 
 Identifier    ZNC-1993-48c-0185 
 Volume    48 
15Author    Andreas Rabenstein, Jörg Rethmeier, Ulrich FischerRequires cookie*
 Title    Sulphite as Intermediate Sulphur Compound in Anaerobic Sulphide Oxidation to Thiosulphate by Marine Cyanobacteria  
 Abstract    Anaerobic sulphide oxidation in the light was studied with seven cyanobacterial strains isolated from the southern Baltic Sea. All strains oxidized sulphide (1.2-3.5 mM) stoichio-metrically to thiosulphate. No elemental sulphur could be detected as end product of anoxy-genic photosynthesis. Sulphite as intermediate sulphur compound was released into the growth medium during anaerobic sulphide oxidation by these cyanobacteria. The formation of sulphite from sulphide was inhibited by the photosynthesis inhibitor DCMU. The cyanobacterium Oscillatoria sp. strain BO 32 produced another so far not identified interm ediate sulphur compound which was probably stored within the cells. 
  Reference    Z. Naturforsch. 50c, 769—774 (1995); received July 24/August 28 1995 
  Published    1995 
  Keywords    Cyanobacteria, Anaerobic Sulphide Oxidation, Interm ediate Sulphur Compounds 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0769.pdf 
 Identifier    ZNC-1995-50c-0769 
 Volume    50 
16Author    Friedrich JüttnerRequires cookie*
 Title    The Algal Excretion Product, Geranylacetone: A Potent Inhibitor of Carotene Biosynthesis in Synechococcus  
 Abstract    The algal excretion product geranylacetone was proved to be an effective and novel inhibitor of carotene synthesis in Synechoccus 6911. The application of geranylacetone resulted in an ac­ cumulation of phytofluene, indicating an inhibition of the conversion of this compound into f-carotene. The cts-isomer of geranylacetone was as effective as the natural irans-isomer. The chloro­ phyll synthesis was only slightly affected. 
  Reference    Z. Naturforsch. 34c, 957 (1979); received June 16 1979 
  Published    1979 
  Keywords    Geranylacetone, Cyanobacteria, Synechococcus, Algal Excretion Product, Inhibitor, Carotene Bio­ synthesis 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0957.pdf 
 Identifier    ZNC-1979-34c-0957 
 Volume    34 
17Author    Irene Alpes, Erwin Stiirzl, Siegfried Scherer, Peter BögerRequires cookie*
 Title    Interaction of Photosynthetic and Respiratory Electron Transport in Blue-Green Algae: Effect of a Cytochrome c-553 Specific Antibody  
 Abstract    An antibody prepared against purified cytochrom e c-553 from Nostoc muscorum inhibits the redox function o f cytochrome c-553 as checked by a diaphorase assay. 20 to 30% inhibition o f NADPH-driven respiratory and light-induced oxygen uptake by Nostoc thylakoids is observed when cytochrome c-553 specific antibodies were applied. H owever, only 30 to 50% o f the total cytochrome c-553 content is released from isolated m em brane m aterial, thus being accessible to antibodies. Supplementing the isolated m embrane m aterial w ith excess Nostoc cytochrom e before adding the antibody abolishes inhibition. The data provide further evidence for soluble cytochrome c-553 being a link between photosynthetic and respiratory electron transport in blue-green algae. 
  Reference    Z. Naturforsch. 39c, 623 (1984); received March 13 1984 
  Published    1984 
  Keywords    Antibody, Cytochrome c-553, Blue G reen-Algae, Cyanobacteria, Interaction Photosynthesis/Respiration 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0623.pdf 
 Identifier    ZNC-1984-39c-0623 
 Volume    39 
18Author    EugeneL. Barsky, FainaD. Kamilova, VitalyD. Samuilov, IcrobiologyRequires cookie*
 Title    Do Cyanobacteria Contain a Membrane Bound Cysteine Oxidase? Department o f Cell Physiology and Im m unology* and Department o f M  
 Abstract    The oxidation o f cysteine with 0 2 is facilitated by isolated membranes o f the cyanobacteria A nacystis nidulans and Anabaena variabilis, and further stimulated by Fe3+. This reaction accelerates with increasing the pH value and is suppressed by cyanide, benzylhydroxamate, hydroxylamine, but not azide. The agents m entioned inhibited the respiration o f the m embranes with ascorbate and N ,N ,N',N'-tetram ethyl-p-phenylenediam ine (TM PD) effectively, but did not influence their nonenzym ic oxidation. It is inferred that ascorbate in com bination with TM PD is oxidized via membrane oxidases. Cysteine oxidation apparently proceeds non-enzym atically and is catalyzed by the cations o f heavy metals. 
  Reference    Z. Naturforsch. 40c, 176 (1985); received October 2/D ecem ber 18 1984 
  Published    1985 
  Keywords    Cysteine Oxidation, Oxygen Uptake, Heavy Metal Cations, Membranes, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0176.pdf 
 Identifier    ZNC-1985-40c-0176 
 Volume    40 
19Author    WimF J Vermaas, JohnG K Williams, CharlesJ. ArntzenRequires cookie*
 Title    Site-Directed Mutations of Two Histidine Residues in the D 2 Protein Inactivate and Destabilize Photosystem II in the Cyanobacterium Synechocystis 6803  
 Abstract    Site-directed m utations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues o f the photosystem II (PS II) D 2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did not show any low-tem perature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. A nother PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role o f the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D 2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous func­ tions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with Q A and Fe:+. In absence o f a functional D 2 protein, the PS II core com plex appears to be destabilized as evidenced by loss o f chlorophyll-proteins in the mutants. 
  Reference    Z. Naturforsch. 42c, 762—768 (1987); received D ecem ber 30 1986 
  Published    1987 
  Keywords    Site-D irected M utagenesis, Herbicide Binding, Photosystem II Proteins, Photosynthesis, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0762.pdf 
 Identifier    ZNC-1987-42c-0762 
 Volume    42 
20Author    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