被氰化物从黄嘌呤氧化酶中释放出的硫原子的性质。35S取代后电子顺磁共振光谱学的证据。
The nature of the sulphur atom liberated from xanthine oxidase by cyanide. Evidence from e.p.r. spectroscopy after 35S substitution.
作者信息
Malthouse J P, Bray R C
出版信息
Biochem J. 1980 Oct 1;191(1):265-7. doi: 10.1042/bj1910265.
Abstract
Active xanthine oxidase was labelled specifically with 33S in the cyanide-labile site of the molybdenum centre. The Very Rapid molybdenum (V) e.p.r. signal, generated from this, shows strong coupling of 33S to molybdenum, providing unambiguous evidence that, at least in the signal-giving species, this sulphur atom is a ligand of molybdenum. The structure of the signal-giving species is discussed.
摘要
活性黄嘌呤氧化酶在钼中心的氰化物敏感位点被33S特异性标记。由此产生的极快的钼（V）电子顺磁共振信号显示33S与钼有强烈的耦合，这提供了明确的证据，表明至少在产生信号的物种中，这个硫原子是钼的配体。文中讨论了产生信号的物种的结构。
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