Role of the Bridging Histidyl Imidazolate Ligand in Yeast Copper-Zinc Superoxide Dismutase. Characterization of the His63Ala Mutant
- 1 October 1994
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 116 (21) , 9743-9744
- https://doi.org/10.1021/ja00100a047
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
- The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity.Proceedings of the National Academy of Sciences, 1988
- Examination of the role of arginine-143 in the human copper and zinc superoxide dismutase by site-specific mutagenesis.Journal of Biological Chemistry, 1987
- 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
- The pH dependence of metal ion binding to the native zinc site of bovine erythrocuprein (superoxide dismutase)Journal of the American Chemical Society, 1982
- 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
- Preparation and characterization of met apo hemocyanin: A single copper(II) active siteBiochemical and Biophysical Research Communications, 1978