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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
    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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  • 3
    Electronic Resource
    Electronic Resource
    1H 3D NOE-NOE spectrum of met-cyanomyoglobin: The first 3D NMR spectrum of a paramagnetic protein (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S3 
    Details
    ISSN: 0749-1581
    Keywords: 1H NMR ; 3D NOE-NOE ; Met-cyanomyoglobin ; Paramagnetic proteins ; Haem proteins ; Iron(III) ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A 3D NOE-NOE spectrum of the paramagnetic protein met-cyanomyoglobin has been successfully obtained. The protein shows hyperfine shifted signals. Planes at their frequencies show clean cross peaks with signals of nearby protons. Connectivities can be detected in-plane at frequencies corresponding to hyperfine broadened signals beneath the diamagnetic envelope, whose connectivities may be difficult to observe otherwise. The limits of observability of cross peaks are discussed by means of spectral simulations.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260311304
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