Magnetic circular dichroism of cobalt-copper and zinc-copper bovine superoxide dismutase.

Abstract The magnetic circular dichroism of the d-d transitions of Co(II) when substituted for Zn(II) in the Zn(II)-Cu(II) enzyme bovine superoxide dismutase enzyme is reported. Magnetic circular dichroism of the Co(II) chromophore in the Co(II)-Cu(II) enzyme is typical of tetrahedral Co(II) compounds. The magnetic circular dichroism band pattern is almost identical with the magnetic circular dichroism of the anion complexes of Co(II) carbonic anhydrase, implying similar coordination geometries in the two enzyme Co(II) complexes. The Cu(II) chromophore is only weakly induced by the magnetic field, with induced ellipticity an order of magnitude less than that of the Co(II) chromophore. Reduction of the Co(II)-Cu(II) protein causes minor, but significant, changes in the Co(II) site as measured by magnetic circular dichroism.

• Publication year

  1973

• Venue

  Journal of Biological Chemistry

• Publication date

  1973-06-10

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0021-9258(19)43813-1PMID 4196587
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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