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  • Articles: DFG German National Licenses  (4)
  • 1H NMR  (2)
  • solution structure  (2)
  • 1
    Electronic Resource
    Electronic Resource
    A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase (1994)
    Springer
    European biophysics journal 23 (1994), S. 167-176 
    Details
    ISSN: 1432-1017
    Keywords: Cu ; Zn ; Superoxide Dismutase ; 1H NMR ; Monomeric analog
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract A mutated protein of human Cu(II)2Zn(II)2 SOD in which residues Phe50 and Gly51 at the dimer interface were substituted by Glu's, thus producing a monomeric species, has been characterized by electronic absorption spectroscopy, EPR, relaxivity and1H NMR techniques. Such substitutions and/or accompanying remodeling and exposure of the dimer interface to solvent, alter the geometry of the active site: increases in the axiality of the copper chromophore and the Cu-OH2 distance have been observed. The affinity of both metal binding sites for Co(II) is also altered. The observed NMR parameters of the Co(II) substituted derivative have been interpreted as a function of the decrease of rotational correlation time as a consequence of the lower molecular weight of the mutated protein. Sharper NMR signals are also obtained for the reduced diamagnetic enzyme. Results are consistent with an active site structure similar to that observed for the dimeric analog Thr137Ile characterized elsewhere. An observed proportional decrease in enzymatic activity and affinity for the N3-anion suggests the importance of electrostatic forces during substrate docking and catalysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01007608
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The auto-orientation in high magnetic fields of oxidized cytochrome b562 as source of constraints for solution structure determination (2000)
    Springer
    Journal of biomolecular NMR 17 (2000), S. 295-304 
    Details
    ISSN: 1573-5001
    Keywords: cytochromes ; magnetic susceptibility anisotropy ; paramagnetism ; residual dipolar couplings ; solution structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract 15N-1H 1J couplings were measured at 500 MHz and 800 MHz for 15N enriched oxidized cytochrome b 562 from E. coli. The magnetic field dependence of 70 1J values, which could be measured without signal overlap, shows that there is a molecular magnetic anisotropy which provides partial molecular orientation in the magnetic field and, consequently, residual dipolar couplings (rdc). The rdc were used as further constraints to improve the existing structure [Arnesano et al. (1999) Biochemistry, 38, 8657–8670] with a protocol which uses the rhombic anisotropy [Banci et al. (1998) J. Am. Chem. Soc., 120, 12903–12909]. The overall large molecular magnetic anisotropy has been found to be determined by both the low spin iron (III) and the four helix bundle structure magnetic susceptibility anisotropy contributions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008308501053
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Paramagnetic relaxation as a tool for solution structure determination: Clostridium pasteurianum ferredoxin as an example (1997)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 29 (1997), S. 348-358 
    Details
    ISSN: 0887-3585
    Keywords: ferredoxin ; NMR ; paramagnetic ; relaxation ; solution structure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The possibility of using the relaxation properties of nuclei for solution structure determination of paramagnetic metalloproteins is critically evaluated. First of all, it is theoretically and experimentally demonstrated that magnetization recovery in non-selective inversion recovery experiments can be approximated to an exponential in both diamagnetic and paramagnetic systems. This permits the estimate of the contribution of paramagnetic relaxation when dominant or sizable. Then, it is shown that the averaging of paramagnetic relaxation rates due to cross relaxation is often tolerably small with respect to the use of paramagnetic relaxation rates as constraints for structural determination. Finally, a protocol is proposed to use such paramagnetic relaxation rates, which depend on the sixth power of the metal to resonating nucleus distance, as constraints for solution structure determination of proteins. As an example, the available solution structure of the oxidized ferredoxin from Clostridium pasteurianum has been significantly improved in resolution especially in the proximity of the metal ions by using 69 new constraints based on paramagnetic relaxation. Proteins 29:348-358, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 4
    Electronic Resource
    Electronic Resource
    Copper-cobalt superoxide dismutase: A re-examination of the 1H NMR spectrum through a novel selectively deuteriated derivative (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S17 
    Details
    ISSN: 0749-1581
    Keywords: 1H NMR ; Copper-cobalt dismutase ; 1D-NOESY ; 2D-NOESY ; T1 measurements ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Through 1D and 2D NOESY experiments, samples of copper-cobalt superoxide dismutase in which the histidines had been completely deuteriated except for the β-CH2 protons were investigated. In this way a simplified spectrum was obtained which allowed the detection of the His NHs of the cobalt domain and their assignment through the kinetics of the proton-deuterium exchange. Further, the β-CH2 protons of Asp 83 were stereospecifically assigned through T1 measurements. Some backbone protons were also assigned.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260311306
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    Paper (German National Licenses)
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