STAFF PRIORITY TIME MOLYBDENUM SITE OF SULFITE OXIDASE

钼和硫K边的X射线吸收光谱 已被用于探测野生型和半胱氨酸207的活性位点。 丝氨酸突变型人亚硫酸盐氧化酶。 的活性中心结构 已经比较了氧化的（静止的）Mo（VI）酶。 的 野生型酶在1.71 E处具有两个Mo=O配体 和三个Mo-S配体在2.41E.这种突变酶具有一种新的 在1.74 E处具有三个Mo=O配体和两个Mo-S的三氧代钼位点 配体在2.47 E.这项工作表明，半胱氨酸207是一个配体的 钼在野生型人亚硫酸盐氧化酶，并在突变体 Mo连接到额外的氧代基团，而不是连接到 取代丝氨酸207。 这篇文章发表于：J。 Chem. 1996，118，8588-8592

X-ray absorption spectroscopy at the molybdenum and sulfur K-edges has been used to probe the active site of wild-type and cysteine 207 . serine mutant human sulfite oxidases. The active site structures of the oxidized (resting) Mo(VI) enzymes have been compared. The wild-type enzyme has been shown to possess two Mo=O ligands at 1.71 E and three Mo-S ligands at 2.41 E. The mutant enzyme possesses a novel tri-oxo molybdenum site with three Mo=O ligands at 1.74 E and two Mo-S ligands at 2.47 E. This work shows that cysteine 207 is a ligand of molybdenum in wild-type human sulfite oxidase, and that in the mutant the Mo is ligated to an extra oxo group rather than to the hydroxyl of the substituant serine 207. This work has been published: J. Am. Chem. Soc. 1996, 118, 8588-8592