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'Cyanide' in keywords
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1Author    Requires cookie*
 Title      
 Abstract    The parameters of complete X-ray struc­ ture determinations are given for the fluorides R b2N aF eF 6 and R b2K F eF 6 (cubic), Cs2NaCrF6 and Cs2N aF eF 6 (hexagonal-rhom-bohedral) and Cs2LiGaF6 (hexagonal). Space group and lattice constants of the monoclinic cyanides Cs2BFe(C N)6 (B = Na, K, Rb) are reported as well. 
  Reference    (Z. Naturforsch. 30b, 462—464 [1975]; eingegangen am 27. Februar 1975) 
  Published    1975 
  Keywords    Fluorides, Cyanides, Structure Determination 
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 TEI-XML for    default:Reihe_B/30/ZNB-1975-30b-0462_n.pdf 
 Identifier    ZNB-1975-30b-0462_n 
 Volume    30 
2Author    Andreas Komath, Oliver BlecherRequires cookie*
 Title    Kristallstruktur und thermische Phasenumwandlung von Tetramethylammoniumcyanid, (Ct^^N+CN- Crystal Structure and Thermal Phase Transition of Tetramethylammonium Cyanide, (CH3)4N+CN~  
 Abstract    Tetramethylammonium cyanide crystallizes in the tetragonal space group P4/nmm, Z = 2, with cell dimensions a = 773.6(1), c = 546.8(1) pm. The cyanide ion is disordered in the plane perpendicular to the c-axis indicating a rotation. The room temperature phase undergoes a thermal phase transition at -59.9°C probably caused by an order-disorder transition of the cyanide ion. 
  Reference    Z. Naturforsch. 54b, 372—376 (1999); eingegangen am 3. November 1998 
  Published    1999 
  Keywords    Cyanides, Crystal Structure, Thermal Phase Transition 
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 TEI-XML for    default:Reihe_B/54/ZNB-1999-54b-0372.pdf 
 Identifier    ZNB-1999-54b-0372 
 Volume    54 
3Author    LeszekA. KleczkowskiRequires cookie*
 Title    Kinetics and Regulation of the NAD(P)H-Dependent Glyoxylate-Specific Reductase from Spinach Leaves  
 Abstract    Kinetic mechanism of purified spinach leaf NAD(P)H glyoxylate reductase (GR-1) was studied using either NADPH and NADH as alternative substrates with glyoxylate. The mech­ anism was elucidated from substrate kinetic patterns using NADH as a cofactor rather than NADPH. With NADPH varied versus glyoxylate, and with NADPH and glyoxylate varied at a constant ratio, the patterns obtained on double reciprocal plots appeared to be consistent with a ping-pong mechanism; however, kinetic patterns with NADH conclusively ruled out the ping-pong reaction in favour of the sequential addition of the reactants. Product inhi­ bition studies with glycolate and NADP have suggested either that NADPH binds to the enzyme before glyoxylate or that the addition of substrates is a random one. Studies with active group modifiers suggested an involvement of histidine, serine and cysteine residues in GR-1 activity. Salts had little or no effect on the activity of the enzyme, with the exception of cyanide, which had an apparent K, of ca. 2 m M . Studies with several metabolites used as possible effectors of GR-1 activity have suggested that the enzyme is modulated only by substrate availability in vivo. The apparent insensitivity of GR-1 to metabolic effectors is consistent with the proposed role of the enzyme in detoxifying glyoxylate which may act as a potent inhibitor of photosynthetic processes in plant tissues. 
  Reference    Z. Naturforsch. 50c, 21—28 (1995); received October 21/November 21 1994 
  Published    1995 
  Keywords    Alternative Substrate, Cyanide, Cytosol, Glycolate Pathway, Glyoxylate Reductase 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0021.pdf 
 Identifier    ZNC-1995-50c-0021 
 Volume    50