Hill H A, Lee W K, Bannister J V, Bannister W H
Biochem J. 1980 Jan 1;185(1):245-52. doi: 10.1042/bj1850245.
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.
报道了人红细胞超氧化物歧化酶(EC 1.15.1.1)的铜(II)/锌(II)、铜(I)/锌(II)和脱辅基形式的170兆赫质子核磁共振谱。共振峰归属于活性位点中组氨酸残基的C-2和C-4质子,并且表明在酶的每个亚基中有五个或六个组氨酸残基作为金属离子的配体。其余已归属的共振峰与组氨酸-41、N端N-乙酰基、组氨酸-108和半胱氨酸-109有关。人和牛超氧化物歧化酶的核磁共振谱比较表明存在显著的结构同源性。