Johnson J L, Rajagopalan K V
Bioinorg Chem. 1978;8(5):439-44. doi: 10.1016/s0006-3061(00)80278-1.
Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at g = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.
亚砷酸盐对鸡肝黄嘌呤脱氢酶的失活作用通过g = 1.97处的钼电子顺磁共振信号得以体现。亚砷酸盐光谱显示出额外的分裂和显著的展宽，但总强度仍与天然酶相当。在存在嘌呤型底物或抑制剂的情况下，可观察到亚砷酸盐处理过的酶的钼信号有进一步的细微变化。
