An extended X-ray-absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase.

N. J. Blackburn, S. S. Hasnain, G. P. Diakun, P. F. Knowles, N. Binsted, C. D. Garner

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Copper and zinc K-edge-extended X-ray-absorption fine structures were measured for the metal sites of freeze-dried bovine superoxide dismutase and the model compounds tetrakis(imidazole)cupric nitrate and tetrakis(imidazole)zinc perchlorate. Detailed simulation of the spectra indicates that the copper site of the enzyme is best fit by co-ordination of four imidazole groups with Cu-N(alpha) distances of 0.198 nm (1.98 A). The zinc site is best fit by three imidazole groups at 0.201 nm (2.01 A) and an oxygen (from aspartate) at 0.203 nm (2.03 A).

Original languageEnglish (US)
Pages (from-to)765-768
Number of pages4
JournalThe Biochemical journal
Volume213
Issue number3
DOIs
StatePublished - Sep 1 1983

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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