A pH-dependent superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein
- 1 January 1982
- journal article
- research article
- Published by Elsevier in Journal of Inorganic Biochemistry
- Vol. 17 (4), 325-341
- https://doi.org/10.1016/s0162-0134(00)80093-8
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Anion binding to the four-copper form of bovine erythrocyte superoxide dismutase: mechanistic implicationsBiochemistry, 1981
- Cadmium-113 nuclear magnetic resonance studies of cadmium-substituted derivatives of bovine superoxide dismutaseBiochemistry, 1980
- pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutaseProceedings of the National Academy of Sciences, 1979
- The binding of copper ions to copper-free bovine superoxide dismutase. Kinetic aspectsBiochemical Journal, 1978
- The involvement of the bridging imidazolate in the catalytic mechanism of action of bovine superoxide dismutaseBiochemical Journal, 1977
- Metal sites of copper-zinc superoxide dismutaseBiochemistry, 1977
- A consideration of the effects of added solutes on the activity of bovine superoxide dismutaseBiochemical Journal, 1977
- The role of the superoxide anion as a toxic species in the erythrocyteArchives of Biochemistry and Biophysics, 1977
- A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamineAnalytical Biochemistry, 1976