赖氨酸化学修饰的铜锌超氧化物歧化酶中阴离子结合和阴离子抑制作用降低，而铜位点的菱形畸变未改变。

Reduced anion binding and anion inhibition in Cu, Zn superoxide dismutase chemically modified at lysines without alteration of the rhombic distortion of the copper site.

作者信息

Cocco D, Mavelli I, Rossi L, Rotilio G

出版信息

Biochem Biophys Res Commun. 1983 Mar 29;111(3):860-4. doi: 10.1016/0006-291x(83)91378-5.

Abstract

The spectroscopic binding constant (visible absorption and EPR spectra) and the catalytic inhibition constant of N-3 and CN- were measured for bovine Cu, Zn superoxide dismutase chemically modified at all lysines by either succinylation or carbamoylation. These modifications partially inactivate the enzyme (10% and 50% residual activity respectively) but leave the native rhombic geometry of the copper site unaffected. It could thus be shown that the observed reduction of anion affinity of the lysines-modified proteins is related to the decreased positive charge of the protein.

摘要

测定了通过琥珀酰化或氨甲酰化对所有赖氨酸进行化学修饰的牛铜锌超氧化物歧化酶的光谱结合常数（可见吸收光谱和电子顺磁共振光谱）以及N-3和CN-的催化抑制常数。这些修饰使酶部分失活（分别残留10%和50%的活性），但铜位点的天然菱形几何结构未受影响。因此可以表明，观察到的赖氨酸修饰蛋白阴离子亲和力的降低与蛋白正电荷的减少有关。