The Interaction of Arsenite with the Molybdenum Center of Chicken Liver Xanthine Dehydrogenase

Jean L. Johnson, K.V. Rajagopalan
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引用次数: 13

Abstract

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.

亚砷酸盐与鸡肝黄嘌呤脱氢酶钼中心的相互作用
亚砷酸盐对鸡肝黄嘌呤脱氢酶的失活作用反映在钼电子顺磁共振信号g = 1.97处。亚砷酸盐光谱显示出额外的分裂和相当大的拓宽,但在总强度上仍与本地相当。在嘌呤型底物或抑制剂的存在下,亚砷酸盐处理酶的钼信号的进一步细微变化可见。
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