Asymmetric active site structures in yeast copper,zinc superoxide dismutase. 1. Reconstruction of apo-superoxide dismutase
- 11 September 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (19) , 4324-4329
- https://doi.org/10.1021/bi00314a011
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Spectroscopic studies of copper(II) bound at the native copper site or substituted at the native zinc site of bovine erythrocuprein (superoxide dismutase)Journal of the American Chemical Society, 1982
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982
- Kinetics of metal dissociation in the yeast Cu2,Zn2-superoxide dismutase. Apparent asymmetry in the metal binding sitesCarlsberg Research Communications, 1982
- Preparation of selectively metal-free and metal-substituted derivatives by reaction of Cu-Zn superoxide dismutase with diethyldithiocarbamateBiochemical Journal, 1981
- Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutaseBiochemistry, 1980
- Cadmium-113 nuclear magnetic resonance studies of cadmium-substituted derivatives of bovine superoxide dismutaseBiochemistry, 1980
- Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopyBiochemical Journal, 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
- Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutasesBiochemistry, 1979
- Nuclear magnetic resonance and chemical modification studies of bovine erythrocyte superoxide dismutase: evidence for zinc-promoted organization of the active site structureBiochemistry, 1977