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

Autor: McAdam, M E, Feilden, E M, Lavelle, F, Calabrese, L, Cocco, D, Rotilio, G
Zdroj: Biochemical Journal; October 1977, Vol. 167 Issue: 1 p271-274, 4p
Abstrakt: 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.
Databáze: Supplemental Index