ZfN: Search Results

1	Author	W. Olfhart Rüdiger, Thom As Brandlmeier, Inge Bios, Jens-Peter Gossauer, Weller	Requires cookie*
	Title	Isolation of the Phytochrome Chromophore. The Cleavage Reaction with Hydrogen Bromide A lbert
	Abstract	The cleavage o f the bilin chromophore from C-phycocyanin with hydrogen bromide yields 3E-configurated phycocyanobilin (4) as the major and 3 Z-configurated phycocyanobilin (5) as the minor reaction product. The reaction o f synthetic 3E-configurated phytochromobilin (2) with hydrogen bromide and methanol leads only to a methanol adduct at the C-18 side chain (7) whereas the same reaction with the 3Z-configurated phytochromobilin (3) leads to 7 and 2. The bilin chromophore was cleaved also from phytochrome after preparation o f phytochromobilin peptides. The detection o f 2 and 7 suggested that 3Z-and 3E-configurated phytochromobilin were the primary products o f cleavage from phytochrome. A reaction scheme is given which can explain the results o f the reaction with hydrogen bromide and methanol.
	Reference	Z. Naturforsch. 35c, 763—769 (1980); received July 11 1980
	Published	1980
	Keywords	Phytochrome, Bile Pigments, Phytochromobilin, Thioether Cleavage, C-Phycocyanin
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	TEI-XML for	default:Reihe_C/35/ZNC-1980-35c-0763.pdf
	Identifier	ZNC-1980-35c-0763
	Volume	35

2	Author	Ahlert Schmidt, Ingrid Erdle, Hans-Peter Köst	Requires 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

3	Author	Fritz Thümmler, W. Olfhart Rüdiger, Edmund Cmiel, Siegfried Schneider	Requires cookie*
	Title	Chromopeptides from Phytochrome and Phycocyanin. NM R Studies o f the Pfr and P r Chromophore of Phytochrome and EyZ Isomeric Chromophores of Phycocyanin
	Abstract	Chromopeptides were prepared by pepsin digestion of C-phycocyanin isolated from the cyano bacterium Spirulina m axim a and o f phytochrom e isolated from seedlings o f Avena sativa L. The chromopeptides were characterized by am ino acid analysis. The Z Z Z configurated chrom ophore of the phycocyanin peptide was transformed into its Z Z E configurated isom er by the m ethod of Falk et al. (Mh. C hem ie 111, 159—175, 1980) which had previously been applied to biliverdins. The 500 MHz 'H N M R spectrum o f the Z Z E configurated chrom opeptides confirmed that its chromophore has the 15 E configuration. Irradiation yielded the Z Z Z configurated isom er for which the 'H N M R spectrum was also recorded. N ative phytochrom e was irradiated at 660 nm to yield the maximum am ount of the Pfr from (about 75% of total phytochrome). By digestion in the dark the previously described Pfr chrom opeptide was obtained. The 500 MHz 'H N M R spectrum was com pared with that o f the Z Z E phycocyanin peptide. It confirmed the 15 £ con figuration of the Pfr chrom opeptide. Irradiation yielded the 15 Z configurated Pr chrom opeptide. Comparison of the high resolution 'H N M R spectra o f Pfr and Pr chrom opeptides revealed that not only the chrom ophore resonances but also those of some amino acids are changed by the Pfr -*■ Pr chrom opeptide phototransform ation. The results are discussed in term s of chrom ophore amino acid interaction.
	Reference	Z. Naturforsch. 38c, 359 (1983); received February 2 1983
	Published	1983
	Keywords	Bilipeptides, C-Phycocyanin, High Resolution N M R Spectra, Photoisom erization, Phytochrom e
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	TEI-XML for	default:Reihe_C/38/ZNC-1983-38c-0359.pdf
	Identifier	ZNC-1983-38c-0359
	Volume	38