Studies on the reconstitution of bovine erythrocyte superoxide dismutase: III. Evidence for a strong interdependence between Cu2+ and Zn2+ binding in the expression of the spectroscopic properties of the native protein and for a close proximity of the Zn2+ and Cu2+ sites
- 25 January 1973
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 295 (1) , 107-116
- https://doi.org/10.1016/0005-2795(73)90078-0
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
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- Studies on the reconstitution of bovine erythrocyte superoxide dismutase: I. The presence of four divalent metal-binding sites on the apo protein which are different from the native sitesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significanceBiochemistry, 1972
- Monomer and magnetic dipole‐coupled Cu2+ EPR signals in nitrosylhemocyaninFEBS Letters, 1972
- Anion Binding to Bovine Erythrocyte Superoxide DismutasePublished by Elsevier ,1972
- Electron spin resonance studies of copper(II) hydroxy-carboxylic acid chelates in aqueous and non-aqueous solutionsJ. Chem. Soc. A, 1969