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1H NMR investigation of reduced copper-cobalt superoxide dismutase

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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.

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Abbreviations

WEFT:

water eliminated Fourier transform

NOE:

nuclear Overhauser effect

NOESY:

NOE spectroscopy

COSY:

correlation spectroscopy

TOCSY:

total correlation spectroscopy

SOD:

superoxide dismutase

E2Co(II)SOD:

SOD with empty copper site (E=empty) and with cobalt(II) in the Zinc(II) site

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Authors and Affiliations

  1. Department of Chemistry, University of Florence, Via G. Capponi 7, I-50121, Florence, Italy

    Ivano Bertini, Mario Piccioli, Margarita Vicens Oliver & Maria Silvia Viezzoli

  2. Institute of Agricultural Chemistry, University of Bologna, Bologna, Italy

    Bertini Luchinat

Authors
  1. Ivano Bertini
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  2. Bertini Luchinat
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  3. Mario Piccioli
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  4. Margarita Vicens Oliver
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  5. Maria Silvia Viezzoli
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Bertini, I., Luchinat, B., Piccioli, M. et al. 1H NMR investigation of reduced copper-cobalt superoxide dismutase. Eur Biophys J 20, 269–279 (1991). https://doi.org/10.1007/BF00450562

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  • DOI: https://doi.org/10.1007/BF00450562

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