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  • 1
    Electronic Resource
    Electronic Resource
    1H NMR studies of the Fe7S8 ferredoxin from Bacillus schlegelii: a further attempt to understand Fe3S4 clusters (1996)
    Springer
    JBIC 1 (1996), S. 523-528 
    Details
    ISSN: 1432-1327
    Keywords: Key words Ferredoxin ; Iron-sulfur clusters ; NMR ; Hyperfine shifts ; Magnetic interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The oxidized Fe7S8 ferredoxin from Bacillus schlegelii, containing both [Fe3S4]+ and [Fe4S4]2+ clusters, has been investigated by 1H NMR spectroscopy. An extensive sequence-specific assignment of the hyperfine-shifted resonances has been obtained by making use of a computer-generated structural model. The pattern and the temperature dependence of the hyperfine shifts of the β-CH2 protons of the cysteines coordinating the [Fe3S4]+ cluster are rationalized in terms of magnetic interactions between the iron ions. The same approach holds for the hyperfine coupling with 57Fe. It is shown that the magnetic interactions are more asymmetric in Fe7S8 ferredoxins than in Fe3S4 ferredoxins. The NMR non-observability of the β-CH2 protons of coordinated cysteines in the one-electron-reduced form has been discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050087
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  • 2
    Electronic Resource
    Electronic Resource
    Heme methyl 1H chemical shifts as structural parameters in some low-spin ferriheme proteins (1999)
    Springer
    JBIC 4 (1999), S. 515-519 
    Details
    ISSN: 1432-1327
    Keywords: Key words Heme protein ; Nuclear magnetic resonance ; Paramagnetic shifts ; Axial ligand
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The different paramagnetic shifts of the four methyl groups in ferriheme proteins have been described as being due to the effect of the axial ligand nodal plane orientation. An equation, heuristically found and theoretically explained, describing the relation between contact and pseudocontact shifts and the position of the axial ligand(s) has been derived for bis-histidine ferriheme proteins and for cyanide-histidine ferriheme proteins. The values of the heuristic parameters contained in the equations were found by fitting the shifts of bovine cytochrome b 5 and several bis-histidine cytochromes c 3 and histidine-cyanide systems. The agreement between the observed and the calculated shifts was found to be good. Therefore, by taking advantage of this study, information on the position of the axial ligands, that can be used as a constraint for structure determination, can be obtained from the shifts of the methyl protons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050337
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  • 3
    Electronic Resource
    Electronic Resource
    1H-NMR and relaxometry of copper-containing dimers in proteins (1990)
    Springer
    BioMetals 3 (1990), S. 146-150 
    Details
    ISSN: 1572-8773
    Keywords: Copper ; Cobalt ; Nickel ; Superoxide dismutase ; Alkaline phosphatase ; NMR ; Relaxometry ; Nuclear relaxation ; Electronic relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The water-proton nuclear-magnetic-relaxation dispersion profiles have been analyzed for Cu2Zn2-superoxide dismutase (SOD) and Cu2-alkaline phosphatase (AP). The electronic relaxation times are derived, together with structural information. The effect of magnetic coupling with another copper ion in Cu2Cu2SOD and Cu2Cu2AP is discussed. It is shown that the electronic relaxation times of copper(II) essentially do not change. The opposite happens with Cu2Co2SOD, Cu2Co2AP and Cu2Ni2SOD in which fast-relaxing metal ions provide relaxation mechanisms for copper(II) as well. In these cases the systems can be studied through high-resolution NMR spectroscopy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01179525
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