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1Author    Günter Döhler, Ralf Barckhausen, Manfred RuppelRequires cookie*
 Title    Ultrastructure of Differently Pigmented Synechococcus Cells  
 Abstract    Synechococcus (.Anacystis nidulans, strain L 1402-1) were grown at + 37 °C in an atmosphere o f 0.04 vol.% C 0 2 using different light conditions. Changing the culture conditions caused alterations in pigment ratios and ultrastructure o f Synechococcus. In comparison to the low white and red light grown cells under strong white light the number o f thylakoids decreased and an accumulation of storage carbohydrates could be observed. The number o f the polyhedral bodies also varied with culture conditions. The results are discussed with reference to the pigment composition and the function of the polyhedral bodies. 
  Reference    Z. Naturforsch. 36c, 907 (1981); received May 15 1981 
  Published    1981 
  Keywords    Synechococcus, Ultrastructure, Polyhedral Bodies, Pigment Composition 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0907_n.pdf 
 Identifier    ZNC-1981-36c-0907_n 
 Volume    36 
2Author    Ahlert Schmidt, Ingrid Erdle, Hans-Peter KöstRequires cookie*
 Title    Changes of C-Phycocyanin in Synechococcus 6301 in Relation to Growth on various Sulfur Compounds Materials and Methods  
 Abstract    The cyanobacterium Synechococcus 6301 is able to use a lim ited number o f sulfur com pounds as the only source o f sulfur supply such as sulfate, thiosulfate, thioacetic acid, m ercaptoacetic acid, thioacetam ide, L-cysteine and glutathione. Com pounds containg thioether linkages such as methionin or S-m ethylcysteine and all com pounds investigated so far containing sulfonic acid structures do not support growth. Growth inhibiton was observed by addition o f am inom ethane-sulfonic acid or cysteamine. When non-growth sustaining sulfur com pounds are added as sulfur source, the C-phycocyanin content o f the Synechococcus cultures decreased drastically, causing a shift in color from blue-green to yellow-green. An analysis reveals the degradation o f C -phycocyanin whereas chlorophyll formation still proceeds to a certain degree in growing sulfur-starved cells. Supplem entation o f a suitable sulfur source induces a period o f intense and preferential C-phycocyanin synthesis prior to resumption o f normal growth. 
  Reference    Z. Naturforsch. 37c, 870—8 (1982); received June 14 1982 
  Published    1982 
  Keywords    Synechococcus, C-Phycocyanin, Sulfur N utrition 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0870.pdf 
 Identifier    ZNC-1982-37c-0870 
 Volume    37 
3Author    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 
4Author    Ahlert SchmidtRequires cookie*
 Title    Occurrence of Mercaptopyruvate Sulfotransferase Activity in Photosynthetic Organisms  
 Abstract    Mercaptopyruvate sulfotransferase activity catalyzes the formation o f pyruvate from mercapto­ pyruvate in the presence o f suitable reagents as acceptor. It was detected in Lemna minor, Pisum sativum, Spinacia oleracea, Chlorella fusca, Synechococcus 6301, and Rhodopseudomonas palustris. Best activity was detected using dithioerythritol as a thiol reagent; good activity was obtained using mercaptoethanol, glutathione, mercaptopyruvate or sulfite as acceptor. The pH-optimum for the Chlorella mercaptopyruvate sulfotransferase was found around 9; the apparent Km for mercaptopyruvate was determined to 2 m M and for dithioerythritol for 5 m M using crude Chlorella extracts. The role of this enzyme is discussed in relation to cysteine catabolism by photosynthetic organisms. 
  Reference    Z. Naturforsch. 39c, 916—921 (1984); received April 6 1984 
  Published    1984 
  Keywords    Pyruvate, Mercaptopyruvate, Lemna, Spinacia, Pisum, Chlorella, Synechococcus, Rhodopseudomonas 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0916.pdf 
 Identifier    ZNC-1984-39c-0916 
 Volume    39 
5Author    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 
6Author    Günter Datz, GünterD. ÖhlerRequires cookie*
 Title    Light-Dependent Changes in the Lipid and Fatty Acid Composition of Phycocyanin-Free Photosynthetic Lamellae of Synechococcus  
 Abstract    The growth o f Synechococcus at different intensities o f white and red light caused changes in the pigment composition. The ratio of chlorophyll a to phycocyanin varied from 1:8,2 in LWLI-grown cells to 1:1,4 in cells grown at HW LI and to 1:15,7 in cultures exposed to HRLI. Acyl lipids were quantitatively determ ined and fatty acids o f the individual lipid classes analysed by GLC. Phycocyanin-free photosynthetic lam ellae were obtained by fractional centrifugation. No variation was found in the acyl lipid composition of the m em brane preparations. These all contained M G D G , D G D G , SQDG and PG as components. In all the lipids investigated, palmitic, hexadecenoic and octadecenoic acids m ade up to more than 90% of total fatty acids. The pattern Of these "m^jor components w ithin the lipids from the different cultures depended on the light used. N o large differences were detected between zones obtained from LWLI and HRLI isolated membranes, whereas density gradient centrifugation of those from HWLI-grown cells resulted in a completely different pattern o f bands. The variations in lipid and fatty acid composition are discussed with respect to changes observed in lipid composition of whole cells and the results reported on tem perature dependent shifts in lipid fluidity in cyanobacteria. 
  Reference    Z. Naturforsch. 36c, 856—862 (1981); recieved May 25 1981 
  Published    1981 
  Keywords    Pigmentation, Phycocyanin-Free Lamellae, Lipid and Fatty Acid Composition, Synechococcus 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0856.pdf 
 Identifier    ZNC-1981-36c-0856 
 Volume    36 
7Author    Divya Mishra, Ahlert SchmidtRequires cookie*
 Title    Regulation and Partly Purification of the ATP-Sulfurylase from the Cyanobacterium Synechococcus 6301  
 Abstract    ATP-sulfurylase from the cyanobacterium Synechococcus 6301 was regulated in vivo during growth in batch culture. The activity was highest at the third day after inoculation, declining afterwards to a level found in resting cells. During growth with air supplemented with 2% CO, this activity increased 3-fold compared to controls grown with normal air as C 0 2 source. Addition o f either nitrite or urea enhanced ATP-sulfurylase activity about 2-fold, whereas cys­ teine and especially methionine decreased ATP-sulfurylase activity to 5% o f controls without treatment. The ATP-sulfurylase was purified by conventional techniques using D EAE-cellulose chro­ matography and further separation on blue sepharose achieving a 250-fold increase in the spe­ cific activity. An apparent o f 5 for APS and o f 40 |iM for pyrophosphate was deter­ mined with the purified enzyme fraction. 
  Reference    Z. Naturforsch. 47c, 95 (1992); received September 26 1991 
  Published    1992 
  Keywords    ATP-Sulfurylase, Cyanobacterium, Synechococcus, Sulfate A ctivation, Regulation 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0095.pdf 
 Identifier    ZNC-1992-47c-0095 
 Volume    47 
8Author    Kazuhiko Satoh, Yasuhiro Kashino, Hiroyuki KoikeRequires cookie*
 Title    Electron Transport from QA to Thymoquinone in a Synechococcus Oxygen-Evolving Photosystem II Preparation: Role of QB and Binding Affinity of Thymoquinone to the QB Site  
 Abstract    We have recently shown that binding affinities o f benzoquinones can be estimated by two methods in photosystem (PS) II particles (K. Satoh et al., Biochim. Biophys. Acta 1 1 0 2 ,4 5 -5 2 (1992)). U sing these methods we calculated the binding affinity o f thym oquinone (2-methyl-5-isopropyl-/?-benzoquinone) to the Q B site and studied how the quinone accepts electrons in oxygen-evolving PS II particles isolated from the thermophilic cyanobacteria, Synechococcus elongatus and S. vulcanus. The results are as follows: (1) The binding constant o f thym oqui­ none to the Q B site determined by several methods was around 0.33 m M . (2) At low thym oqui­ none concentrations the quinone was supposed to accept electrons via QB-plastoquinone, whereas at high concentrations the quinone seemed to bind to the QB site and accept an elec­ tron directly from Q~A. Lower rates o f photoreduction o f the quinone at high concentrations were attributed to a slower turnover rate o f the quinone at the QB site than that o f endogenous plastoquinone. (3) A model for the function o f plastoquinone at the Q B site, which can explain all the results, was presented. According to this model, the plastoquinone molecule at the Q B site is not replaced by another plastoquinone molecule. Instead, it transfers electrons to pool plastoquinone molecules by turning over its head group but remaining its long side chain bound to the PS II complexes. 
  Reference    Z. Naturforsch. 48c, 174 (1993); received November 9 1992 
  Published    1993 
  Keywords    Q b Site, Photosystem II, Thym oquinone, Plastoquinone, Synechococcus 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0174.pdf 
 Identifier    ZNC-1993-48c-0174 
 Volume    48 
9Author    Günter DöhlerRequires cookie*
 Title    Einfluß von Sauerstoff auf die photosynthetische C 0 2-Fixierung von Synechococcus Effect of Oxygen on Photosynthetic C 0 2 Fixation of Synechococcus  
 Abstract    The cyanobacterium Synechococcus (Anacystis nidulans strain L 1402-1) was grown at +35 °C in air and in air enriched with 2.2 vol.% C 0 2. The effect o f different oxygen concentrations (0, 2, 20, 50, 75 and 99.97 or 97.8 vol.%) was studied in low (0.03 vol.%) and high (2.2 vol.%) C 0 2 concentrations at + 35 °C. After exposure to a nitrogen atmosphere and low C 0 2 content I4C-bicarbonate was mainly incorporated into aspartate and glycine/serine. During oxygenic photosynthetic C 0 2 fixation label in aspartate decreased and a high degree o f radioactivity could be found in 3-phosphoglyceric acid and sugar monophosphates. The Calvin cycle was the main fixing pathway in 2.2 vol.% C 0 2 during anoxygenic and oxygenic conditions independent on the 0 2 concentrations during the experiments. N o oxygen enhancement o f photosynthetic C 0 2 fixation could be found. Possible mechanism involved in C 0 2 fixation pathways and glycolate metabolism underlying the effect o f oxygen was discussed. 
  Reference    Z. Naturforsch. 36c, 93—9 (1981); eingegangen am 9. Oktober 1980 
  Published    1981 
  Keywords    14C 0 2 Fixation, Effect of Oxygen and C 0 2 Concentrations, Synechococcus 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0093.pdf 
 Identifier    ZNC-1981-36c-0093 
 Volume    36