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. 1983 Sep 1;213(3):765–768. doi: 10.1042/bj2130765

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
PMCID: PMC1152194  PMID: 6615458

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).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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