Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopy
- 1 January 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 185 (1) , 245-252
- https://doi.org/10.1042/bj1850245
Abstract
The 170MHZ 1 H n.m.r. spectra of the Cu(II)/Zn(II), Cu(I)/Zn(II) and apo- forms of human erythrocyte superoxide dismutase (EC 1.15.1.1) are reported. Resonances are assigned to the C-2 and C-4 protons of histidine residues in the active site, and it is suggested that five or six histidine residues serve as ligands to the metal ions in each subunit of the enzyme. The remaining assigned resonances are associated with histidine-41, N-terminal N-acetyl group, histidine- 108 and cysteine- 109. A comparison of the n.m.r. spectra of human and bovine superoxide dismutases suggests significant structural homology.This publication has 14 references indexed in Scilit:
- Sulfhydryl reactivity of human erythrocyte superoxide dismutaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Further characterization of human erythrocyte superoxide dismutaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutaseBiochemical Journal, 1977
- Investigation of the structure of bovine erythrocyte superoxide dismutase by proton nuclear magnetic resonance spectroscopyBiochemistry, 1977
- Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.Proceedings of the National Academy of Sciences, 1975
- Alpha-carbon coordinates for bovine Cu, Zn superoxide dismutaseBiochemical and Biophysical Research Communications, 1975
- Bovine erythrocyte superoxide dismutase. Complete amino acid sequence.1974
- Studies on the reconstitution of bovine erythrocyte superoxide dismutase. IV. Preparation and some properties of the enzyme in which Co(II) is substituted for Zn(II).1973
- Nuclear magnetic resonance spectra of human and bovine superoxide dismutasesFEBS Letters, 1973
- Preparation of pure bovine apo‐erythrocuprein by gel filtrationFEBS Letters, 1971