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  • crystal structure  (4)
  • Flavodoxin  (3)
  • Springer  (7)
  • International Union of Crystallography
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  • Springer  (7)
  • International Union of Crystallography
  • Elsevier  (2)
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  • 1
    Digitale Medien
    Digitale Medien
    Crystal structure of the Λ-[4M] enantiomer of cis-diaqua-bis(1,3-dimethylpteridine-2,4(1H,3H)-dione-N5,O4) copper(II) perchlorate monohydrate (1999)
    Springer
    Journal of chemical crystallography 29 (1999), S. 571-574 
    Details
    ISSN: 1572-8854
    Schlagwort(e): crystal structure ; complexes ; pteridine ; lumazine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Geologie und Paläontologie , Physik
    Notizen: Abstract Single-crystal X-ray diffraction studies have been performed on the complex cis-diaqua-bis(1,3-dimethylpteridine-2,4(1H,3H)-dione-O4,N5) copper(II) perchlorate monohydrate, [Cu(DLM)2(H2O)2](ClO4)2 · H2O. This compound crystallizes in the orthorhombic system, P212121 space group, Z = 4 with a = 8.749(1) Å, b = 14.213(1) Å, c = 21.200(2) Å, and V = 2636.2(4) Å3. The metal ion is surrounded in octahedral geometry by two mutually quasi-perpendicular N5,O4-coordinated lumazine chelators with the O4 atoms trans and the N5 atoms cis. The polyhedron is completed by two cis-coordinated water molecules. The absolute configuration of the complex can be described, following Bailar's nomenclature, as the enantiomer Λ of the stereoisomer 4M. A three-dimensional hydrogen-bond network is defined by water molecules, perchlorate anions, and the O2 of the pteridine A.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1009548803103
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  • 2
    Digitale Medien
    Digitale Medien
    Synthesis, characterization, and crystal structure of 1,3,7,9-tetramethylpyrido-[2,3-d∶6,5-d′]-dipyrimidine-2,4,6,8-tetrone (1994)
    Springer
    Journal of chemical crystallography 24 (1994), S. 465-468 
    Details
    ISSN: 1572-8854
    Schlagwort(e): Pyrimidine ; uracil ; crystal structure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Geologie und Paläontologie , Physik
    Notizen: Abstract A new and easy method for the preparation of 1,3,7,9-tetramethylpyrido-[2,3-d∶6,5-d′]-dipyrimidine-2,4,6,8-tetrone is described. The structure of this compound has been solved by means of X-ray diffraction methods. The chemical characterization by spectral (mass, ultraviolet, infrared, and proton nuclear magnetic resonance) and thermal (thermogravimetry and differential scanning calorimetry) method is also reported. The compound is monoclinic, space groupP21/c,a=12.720(5),b=13.688(7),c=8.079(2) Å, β=107.06(4)°,Z=4. The structure consists of discrete tricyclic molecules, stacking playing an important role in crystal packing.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01666096
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  • 3
    Digitale Medien
    Digitale Medien
    Crystal structure of a novel tertiary phosphine coordination complex: dichlorobis(tribenzylphosphine)nickel(II) (2000)
    Springer
    Journal of chemical crystallography 30 (2000), S. 173-176 
    Details
    ISSN: 1572-8854
    Schlagwort(e): phosphine ; nickel(II) complexes ; crystal structure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Geologie und Paläontologie , Physik
    Notizen: Abstract The title compound dichlorobis(tribenzylphosphine)nickel(II), Ni[P(CH2C6H5)3]2Cl2, belongs to a type of tertiary phosphine coordination complex, M(PR3)2X2. There are two molecules in the unit cell which do not appear to interact chemically. Both molecules have a trans-square planar configuration with each nickel atom on a center of symmetry. Three benzyl groups are bonded to each phosphorus atom as rotors in a propeller, and the threefold axis is along the P—Ni bond, which has a mean length of 2.23(1) Å. Crystal data: C42H42Cl2NiP2, Triclinic, space group $$P\bar 1 $$ , a = 10.4892(15) b = 10.5249(12) c = 19.453(2) Å, α = 83.872(8), β = 76.839(9), γ = 62.241(8)°, V = 1850.5(4) Å3, Z = 2. There is an intramolecular hydrogen bond between the C3 and C11 atoms.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1009543401270
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  • 4
    Digitale Medien
    Digitale Medien
    Effect of iron deficiency on ferredoxin levels in Anabaena variabilis PCC 6309 (1990)
    Springer
    Archives of microbiology 153 (1990), S. 528-530 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Anabaena ; Ferredoxin ; Flavodoxin ; Iron deficiency
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Cultures of the nitrogen-fixing cyanobacterium Anabaena variabilis PCC 6309 were grown under several iron concentrations, and changes in growth rates and chlorophyll and phycocyanin concentrations were determined. The total amount of ferredoxin present in the cells was found to be dependent on the concentration of iron in the media, as was the pattern distribution of the two different forms of the iron-sulfur protein described in this organism. Flavodoxin was not found to be present in these cells even when they were grown in the absence of added iron, indicating that this flavoprotein does not replace ferredoxin in this particular strain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00245260
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  • 5
    Digitale Medien
    Digitale Medien
    Flavodoxin from the nitrogen-fixing cyanobacterium Anabaena PCC 7119 (1988)
    Springer
    Archives of microbiology 150 (1988), S. 160-164 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Anabaena ; Biochemical properties ; Flavodoxin ; Nitrogenase ; Photosystem-I electron transport ; Spectral characteristics
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Flavodoxin has been isolated and purified from cultures of the cyanobacterium Anabaena cultivated in a low-iron medium. This flavoprotein has a molecular weight of 20,000 and contains 1 molecule of flavin mononucleotide per mol of protein. Various biochemical characteristics are reported including amino-acid composition, isoelectric point and the fluorescence properties of the apoprotein. The extinction coefficients and isosbestic points were determined for the oxidized and semiquinone forms of flavodoxin. The electron paramagnetic resonance spectrum of the semiquinone exhibited a spectral linewidth of 23 G, which is typical for a neutral flavoprotein semiquinone. Kinetic measurements give a rate constant of 9.6×107 (M-1 min-1) for the reduction of flavodoxin in the photosynthetic electron-transport chain by the photosystem I and 6.6×106 for the reaction in which flavodoxin is reduced by ferredoxin-NADP+ oxidoreductase. The Michaelis constant for electron donation to nitrogenase by reduced flavodoxin is 8.5 μM.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00425156
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  • 6
    Digitale Medien
    Digitale Medien
    Ferredoxin-NADP+ reductase uses the same site for the interaction with ferredoxin and flavodoxin (1999)
    Springer
    JBIC 4 (1999), S. 568-578 
    Details
    ISSN: 1432-1327
    Schlagwort(e): Key words Ferredoxin ; Ferredoxin-NADP+ reductase ; Flavodoxin ; Protein-protein interaction
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract  The enzyme ferredoxin-NADP+ reductase (FNR) forms a 1 : 1 complex with ferredoxin (Fd) or flavodoxin (Fld) that is stabilised by both electrostatic and hydrophobic interactions. The electrostatic interactions occur between acidic residues of the electron transfer (ET) protein and basic residues on the FNR surface. In the present study, several charge-reversal mutants of FNR have been prepared at the proposed site of interaction of the ET protein: R16E, K72E, K75E, K138E, R264E, K290E and K294E. All of these mutants have been assayed for reactivity with Fd and Fld using steady-state and stopped-flow kinetics. Their abilities for complex formation with the ET proteins have also been tested. The data presented here indicate that the mutated residues situated within the FNR FAD-binding domain are more important for achieving maximal ET rates, either with Fd or Fld, than those situated within the NADP+-binding domain, and that both ET proteins occupy the same region for the interaction with the reductase. In addition, each individual residue does not appear to participate to the same extent in the different processes with Fd and Fld.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1432-1033.1968.tb00250.x
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  • 7
    Digitale Medien
    Digitale Medien
    Crystal, Molecular, and Electronic Structure of 1-Acetyl-indoline and Derivatives (1998)
    Springer
    Structural chemistry 9 (1998), S. 365-373 
    Details
    ISSN: 1572-9001
    Schlagwort(e): 1-Acetyl-indoline ; crystal structure ; electronic structure ; AM1 calculation ; CI calculation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The crystal and molecular structures of the following molecules have been determined: 1-acetyl-indoline, 1-acetyl-5-nitro-indoline, l-acetyl-5-nitro-7-bromo-indoline, 1-acetyl-5-bromo-7-nitroindoline, and l-acetyl-5-bromo-7-nitro-indol. Molecular orbital calculations are performed for these compounds and two related species.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1022419111660
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