No CrossRef data available.
Article contents
Characterisation by EPR spectroscopy of the co-ordination environment of copper in superoxide dismutase from horseradish (Armoracia rusticana Gaertn.)
Published online by Cambridge University Press: 05 December 2011
Abstract
An abstract is not available for this content so a preview has been provided. Please use the Get access link above for information on how to access this content.

- Type
- Short Communications
- Information
- Copyright
- Copyright © Royal Society of Edinburgh 1994
References
Beem, K. M., Richardson, D. C. & Rajagopalan, K. V. 1977. Metal sites of copper-zinc superoxide dismutase. Biochemistry 16, 1930–7.Google Scholar
Briggs, R. G. & Fee, J. A. 1978. Further characterization of human erythrocyte superoxide dismutase. Biochimica et Biophysica Acta 537, 86–99.Google Scholar
Fielden, E. M., Roberts, P. B., Bray, R. C., Lowe, D. J., Mautner, G. N., Rotilio, G. & Calabrese, L. 1973. The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Biochemical Journal 139, 49–60.Google Scholar
Fridovich, I. 1986. Biological effects of the superoxide radical. Archives of Biochemistry and Biophysics 247, 1–11.CrossRefGoogle ScholarPubMed
Lieberman, R. A., Sands, R. H. & Fee, J. A. 1982. A study of the electron paramagnetic resonance properties of single monoclinic crystals of bovine superoxide dismutase. Journal of Biological Chemistry 257, 336–44.Google Scholar
Tainer, J. A., Getzoff, E. P., Beem, K. M., Richardson, J. S. & Richardson, D. C. 1982. Determination and analysis of the 2A structure of copper, zinc superoxide dismutase. Journal of Molecular Biology 160, 181–217.CrossRefGoogle Scholar