Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 May 1;219(3):985–990. doi: 10.1042/bj2190985

An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme.

N J Blackburn, S S Hasnain, N Binsted, G P Diakun, C D Garner, P F Knowles
PMCID: PMC1153572  PMID: 6743256

Abstract

Copper and zinc K-edge e.x.a.f.s. (extended X-ray-absorption fine structures) were measured for the metal sites of oxidized and reduced bovine superoxide dismutase in aqueous solution. Detailed analysis of the spectra indicates that the copper site of the enzyme changes on reduction and is most probably co-ordinated to three imidazole groups at a shorter distance Cu-N(alpha) = 0.194 nm (1.94 A) in the reduced form compared with a co-ordination of four imidazole groups at 0.199 nm (1.99 A) and an oxygen atom from solvent water at 0.224 nm (2.24 A) in the oxidized form. Examination of the edge, near-edge structure and e.x.a.f.s. of the zinc sites indicates that the stereochemical changes at copper that accompany reduction introduce minimal perturbation on the stereochemistry at zinc.

Full text

PDF
985

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bailey D. B., Ellis P. D., Fee J. A. Cadmium-113 nuclear magnetic resonance studies of cadmium-substituted derivatives of bovine superoxide dismutase. Biochemistry. 1980 Feb 5;19(3):591–596. doi: 10.1021/bi00544a031. [DOI] [PubMed] [Google Scholar]
  2. Blackburn N. J., Hasnain S. S., Diakun G. P., Knowles P. F., Binsted N., Garner C. D. An extended X-ray-absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase. Biochem J. 1983 Sep 1;213(3):765–768. doi: 10.1042/bj2130765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blumberg W. E., Peisach J., Eisenberger P., Fee J. A. Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy. Biochemistry. 1978 May 16;17(10):1842–1846. doi: 10.1021/bi00603a006. [DOI] [PubMed] [Google Scholar]
  4. Boden N., Holmes M. C., Knowles P. F. Properties of the cupric sites in bovine superoxide dismutase studied by nuclear-magnetic-relaxation measurements. Biochem J. 1979 Jan 1;177(1):303–309. doi: 10.1042/bj1770303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fee J. A., DiCorleto P. E. Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase. Biochemistry. 1973 Nov 20;12(24):4893–4899. doi: 10.1021/bi00748a013. [DOI] [PubMed] [Google Scholar]
  6. Fee J. A., Gaber B. P. Anion binding to bovine erythrocyte superoxide dismutase. Evidence for multiple binding sites with qualitatively different properties. J Biol Chem. 1972 Jan 10;247(1):60–65. [PubMed] [Google Scholar]
  7. Fee J. A., Ward R. L. Evidence for a coordination position available to solute molecules on one of the metals at the active center of reduced bovine superoxide di smutase. Biochem Biophys Res Commun. 1976 Jul 26;71(2):427–437. doi: 10.1016/0006-291x(76)90805-6. [DOI] [PubMed] [Google Scholar]
  8. Lawrence G. D., Sawyer D. T. Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases. Biochemistry. 1979 Jul 10;18(14):3045–3050. doi: 10.1021/bi00581a021. [DOI] [PubMed] [Google Scholar]
  9. Lieberman R. A., Sands R. H., Fee J. A. A study of the electron paramagnetic resonance properties of single monoclinic crystals of bovine superoxide dismutase. J Biol Chem. 1982 Jan 10;257(1):336–344. [PubMed] [Google Scholar]
  10. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  11. Perutz M. F., Hasnain S. S., Duke P. J., Sessler J. L., Hahn J. E. Stereochemistry of iron in deoxyhaemoglobin. Nature. 1982 Feb 11;295(5849):535–538. doi: 10.1038/295535a0. [DOI] [PubMed] [Google Scholar]
  12. Richardson J., Thomas K. A., Rubin B. H., Richardson D. C. Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1349–1353. doi: 10.1073/pnas.72.4.1349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Tainer J. A., Getzoff E. D., Beem K. M., Richardson J. S., Richardson D. C. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J Mol Biol. 1982 Sep 15;160(2):181–217. doi: 10.1016/0022-2836(82)90174-7. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES