Properties of the cupric sites in bovine superoxide dismutase studied by nuclear-magnetic-relaxation measurements
- 1 January 1979
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 177 (1) , 303-309
- https://doi.org/10.1042/bj1770303
Abstract
Proton nuclear-relaxation rates have been measured as a function of frequency, temperature, pH and cyanide concentration in aqueous solutions of superoxide dismutase from bovine erythrocytes. The results show that, whereas for pH less than or equal to 9 only one water molecule is bound to each Cu2+ ion, at higher pH a second co-ordination site for OH- becomes available; it is proposed that this involves cleavage of the bond between Cu2+ and the histidine residue that bridges to Zn2+.This publication has 15 references indexed in Scilit:
- Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methodsBiochemical Journal, 1979
- Metal sites of copper-zinc superoxide dismutaseBiochemistry, 1977
- Superoxide DismutasesAnnual Review of Biochemistry, 1975
- 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
- pH dependence of the nuclear magnetic relaxation rate of solvent water protons in solutions of bovine superoxide dismutaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Binding of water to “Types I and II” Cu2+ in proteinsBiochemical and Biophysical Research Communications, 1974
- The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysisBiochemical Journal, 1974
- Metal sites of copper proteins. III. Symmetry of copper in bovine superoxide dismutase and its functional significanceBiochemistry, 1972
- Anion binding to bovine erythrocyte superoxide dismutase. Evidence for multiple binding sites with qualitatively different properties.1972
- Superoxide dismutase: Improved assays and an assay applicable to acrylamide gelsAnalytical Biochemistry, 1971