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. 1977 Oct 1;167(1):271–274. doi: 10.1042/bj1670271

The involvement of the bridging imidazolate in the catalytic mechanism of action of bovine superoxide dismutase.

M E McAdam, E M Feilden, F Lavelle, L Calabrese, D Cocco, G Rotilio
PMCID: PMC1183644  PMID: 588256

Abstract

The pulse-radiolysis method has been used to study the catalytic mechanism of O2 leads to dismutation by the Co(II)-substituted bovine erythrocuprein (superoxide dismutase, EC 1.15.1.1). Catalysis is accompanied by spectral changes that may be interpreted in terms of rapid protonation and deprotonation of the Cu-facing nitrogen atom of the imidazolate that bridges the Cu(II) and the Co(II) [or Zn(II)] in the oxidized enzyme. This rapid change permits the possibility that the imidazole is a proton donor in the catalytic reduction of O2 leads to.

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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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