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• W2325822092 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+." @default.
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• W2325822092 date "1979-01-01" @default.
• W2325822092 modified "2023-09-26" @default.
• W2325822092 title "Properties of the cupric sites in bovine superoxide dismutase studied by nuclear-magnetic-relaxation measurements" @default.
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• W2325822092 doi "https://doi.org/10.1042/bj1770303" @default.
• W2325822092 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1186369" @default.
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