| Literature DB >> 6615458 |
N J Blackburn, S S Hasnain, G P Diakun, P F Knowles, N Binsted, C D Garner.
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).Entities:
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Year: 1983 PMID: 6615458 PMCID: PMC1152194 DOI: 10.1042/bj2130765
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857