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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >myo-Inositol oxygenase: a radical new pathway for O-2 and C-H activation at a nonheme diiron cluster
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myo-Inositol oxygenase: a radical new pathway for O-2 and C-H activation at a nonheme diiron cluster

机译：肌醇加氧酶：在非血红素二铁簇上O-2和C-H活化的根本途径

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摘要

The enzyme myo-inositol oxygenase (MIOX) catalyzes conversion of myo-inositol (cyclohexan-1,2,3,5/4,6-hexa-ol or MI) to D-glucuronate (DG), initiating the only known pathway in humans for catabolism of the carbon skeleton of cell-signaling inositol (poly) phosphates and phosphoinositides. Recent kinetic, spectroscopic and crystallographic studies have shown that the enzyme activates its substrates, MI and O-2, at a carboxylate-bridged nonheme diiron(II/III) cluster, making it the first of many known nonheme diiron oxygenases to employ the mixed-valent form of its cofactor. Evidence suggests that: (1) the Fe(III) site coordinates MI via its C1 and C6 hydroxyl groups; (2) the Fe(II) site reversibly coordinates O-2 to produce a superoxo-diiron(III/III) intermediate; and (3) the pendant oxygen atom of the superoxide ligand abstracts hydrogen from C1 to initiate the unique C-C-bond-cleaving, four-electron oxidation reaction. This review recounts the studies leading to the recognition of the novel cofactor requirement and catalytic mechanism of MIOX and forecasts how remaining gaps in our understanding might be filled by additional experiments.
机译：肌肉肌醇加氧酶（MIOX）催化肌肉肌醇（环己基1,2,3,5,4,6-己醇或MI）转化为D-葡萄糖醛酸酯（DG），从而启动了唯一的已知途径人类对细胞信号肌醇（聚）磷酸酯和磷酸肌醇碳骨架的分解代谢。最近的动力学，光谱和晶体学研究表明，该酶在羧酸桥联的非血红素二铁（II / III）簇上激活其底物MI和O-2，使其成为许多已知的混合使用的非血红素二铁加氧酶中的第一个。辅因子的价形式。有证据表明：（1）Fe（III）位点通过其C1和C6羟基与MI配位; （2）Fe（II）位点可逆地配位O-2以产生超氧二铁（III / III）中间体; （3）超氧化物配体的侧挂氧原子从C1中提取氢，以引发独特的C-C键裂解，四电子氧化反应。这篇综述叙述了导致人们认识到MIOX的新型辅助因子需求和催化机理的研究，并预测了其他实验将如何填补我们理解中的空白。

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