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1995 (1)
1991 (1)
1Author    S. Frenzen, Hk Müller-BuschbaumRequires cookie*
 Title    Uber einen 9L-Perowskit der Zusammensetzung Ba9Ru3? 2Mn5?8027 On a 9L-Perovskite of the Composition Ba9Ru3 2Mn5 80 27  
 Abstract    Single crystals of Ba9Ru3 2Mn5 80 27 have been prepared by flux techniques. X-ray four circle diffractometer measurements led to trigonal (rhombohedral) symmetry, space group D3d-R 3 m , a = 5.7043(5), c = 21.255(4) A , Z = 1. This phase is isotypic to B a R u 0 3. The crystal structure and the occupation of the M3O i2 triple octahedra by ruthenium and manga­ nese are discussed with respect to other oxides containing M30 12 groups in an ordered and disordered way. 
  Reference    Z. Naturforsch. 50b, 585 (1995); eingegangen am 10. Oktober 1994 
  Published    1995 
  Keywords    Barium, Ruthenium, M anganese, Oxide, Perovskite, Structure 
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 TEI-XML for    default:Reihe_B/50/ZNB-1995-50b-0585.pdf 
 Identifier    ZNB-1995-50b-0585 
 Volume    50 
2Author    Bengt Svensson, Imre Vass, Stenbjörn StyringRequires cookie*
 Title    Sequence Analysis of the D 1 and D 2 Reaction Center Proteins of Photosystem II  
 Abstract    A com pilation o f 38 sequences for the D1 and 15 sequences for the D 2 reaction center pro­ teins o f photosystem II is presented. The sequences have been compared and a similarity index that takes into account the degree o f conservation and the quality o f the changes in each posi­ tion has been calculated. The similarity index is used to identify and describe functionally im­ portant domains in the D 1 /D 2 heterodimer. Comparative hydropathy plot are presented for the aminoacid sidechains that constitute the binding domain o f the tyrosine radicals, Tyrz and TyrD, in photosystem II. The structure around Tyrz is more hydrophilic than the structure around TyrD. The hydrophilic residues are clustered in the part o f the binding pocket for Tyrz that is turned towards the lumenal side o f the thylakoid membrane. M ost prominent is the presence o f two conserved carboxylic am inoacids, D l-A sp 170 and D l-G lu 189. Their respec­ tive carboxyl-groups com e close in space and are proposed to constitute a metal binding site together with D l-G ln 165. The distance between the proposed metal binding site and the cen­ ter o f the ring o f Tyrz is approximately 7Ä . The cavity that constitutes the binding site for TyrD is com posed o f residues from the D 2 protein. Its character is more hydrophobic than the Tyrz site and the environment around TyrD lacks the cluster o f putative metal binding side­ chains. 
  Reference    Z. Naturforsch. 46c, 765 (1991); received March 13 1991 
  Published    1991 
  Keywords    Photosystem II, D1 Protein, D 2 Protein, Tyrosine, M anganese, Reaction Center 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0765.pdf 
 Identifier    ZNC-1991-46c-0765 
 Volume    46