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Superoxide-dismutase, a study of electronic properties of copper and zinc by x-ray absorption spectroscopy

Academic Article
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Overview

authors

  • Blumberg, W. E.
  • Peisach, J.
  • Eisenberger, P.
  • Fee, James

publication date

  • 1978

journal

  • Biochemistry  Journal

abstract

  • The x-ray absorption for copper and zinc in oxidized and reduced superoxide dismutase, as well as in various model compounds, was studied. Upon reduction of the protein, the added electron affects the copper site almost exclusively, while the zinc remains virtually unchanged. Reduction decreases the charge on the copper atom [toward Cu(I)] and changes the configuration of the copper site so that it becomes less symmetric. An analysis of the copper absorption observed with the oxidized enzyme and a comparison with that for Cu(II)(imid)4 suggests that the copper is not simply ligated to four imidazoles. The addition of H2O2 to superoxide dismutase reduces the copper to Cu(I), while oxygen addition to the peroxide-reduced protein restores the copper to Cu(II).

subject areas

  • Absorption
  • Animals
  • Cattle
  • Copper
  • Imidazoles
  • Pyridines
  • Spectrum Analysis
  • Superoxide Dismutase
  • X-Rays
  • Zinc
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00603a006

PubMed ID

  • 566111
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Additional Document Info

start page

  • 1842

end page

  • 1846

volume

  • 17

issue

  • 10

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