The involvement of the bridging imidazolate in the catalytic mechanism of action of bovine superoxide dismutase
- 1 October 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 167 (1) , 271-274
- https://doi.org/10.1042/bj1670271
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.This publication has 11 references indexed in Scilit:
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