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  • 1990-1994  (4)
  • 1H NMR  (2)
  • Analytical Chemistry and Spectroscopy  (2)
  • 1HNMR  (1)
  • 1
    Electronic Resource
    Electronic Resource
    1H NMR investigation of reduced copper-cobalt superoxide dismutase (1991)
    Springer
    European biophysics journal 20 (1991), S. 269-279 
    Details
    ISSN: 1432-1017
    Keywords: 1HNMR ; Metal substitution ; Superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Human copper-cobalt superoxide dismutase in the reduced form has been investigated through 1H NMR techniques. The aim is to monitor the structural properties of this derivative and to compare them with those of reduced and oxidized native superoxide dismutases. The observed signals of the cobalt ligands have been assigned as well as the signals of the histidines bound to copper(I). The latter signals experience little pseudocontact shifts which allow a rough orientation of the magnetic susceptibility tensor in the molecular frame. The connectivities indicate that, although the histidine bridge is broken in the reduced form, the interproton distances between ligands of both ions are essentially the same.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00450562
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    Paper (German National Licenses)
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Guest editor's foreword (1993)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S1 
    Details
    ISSN: 0749-1581
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260311302
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    Paper (German National Licenses)
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  • 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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