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首页> 外文期刊>Chemistry: A European journal >Structure and Mechanism Leading to Formation of the Cysteine Sulfinate Product Complex of a Biomimetic Cysteine Dioxygenase Model
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Structure and Mechanism Leading to Formation of the Cysteine Sulfinate Product Complex of a Biomimetic Cysteine Dioxygenase Model

机译：仿生半胱氨酸双加氧酶模型的半胱氨酸亚磺酸产物复合物形成的结构和机理

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摘要

Cysteine dioxygenase is a unique nonheme iron enzyme that is involved in the metabolism of cysteine in the body. It contains an iron active site with an unusual 3-His ligation to the protein, which contrasts with the structural features of common nonheme iron dioxygenases. Recently, some of us reported a truly biomimetic model for this enzyme, namely a trispyrazolylborato iron(II) cysteinato complex, which not only has a structure very similar to the enzyme-substrate complex but also represents a functional model: Treatment of the model with dioxygen leads to cysteine dioxygenation, as shown by isolating the cysteine part of the product in the course of the work-up. However, little is known on the conversion mechanism and, so far, not even the structure of the actual product complex had been characterised, which is also unknown in case of the enzyme. In a multidisciplinary approach including density functional theory calculations and X-ray absorption spectroscopy, we have now determined the structure of the actual sulfinato complex for the first time. The Cys-SO2- functional group was found to be bound in an eta(2)-O,O-coordination mode, which, based on the excellent resemblance between model and enzyme, also provides the first support for a corresponding binding mode within the enzymatic product complex. Indeed, this is again confirmed by theory, which had predicted a eta(2)-O,O-binding mode for synthetic as well as the natural enzyme.
机译：半胱氨酸双加氧酶是一种独特的非血红素铁酶，参与体内半胱氨酸的代谢。它含有一个铁活性位点，与蛋白质的3-His连接异常，这与常见的非血红素铁双加氧酶的结构特征形成鲜明对比。最近，我们中的一些人报道了该酶的真正仿生模型，即三吡唑基硼酸铁（II）半胱氨酸复合物，它不仅具有与酶-底物复合物非常相似的结构，而且还代表了一种功能模型：如在后处理过程中分离出产品的半胱氨酸部分所示，双氧会导致半胱氨酸双氧合。但是，对于转化机理知之甚少，到目前为止，甚至没有表征出实际产物复合物的结构，这在酶的情况下也是未知的。在包括密度泛函理论计算和X射线吸收光谱在内的多学科方法中，我们现在首次确定了实际的磺胺基配合物的结构。发现Cys-SO2-官能团以eta（2）-O，O-配位模式结合，基于模型和酶之间的极好的相似性，它还提供了相应的结合模式的第一个支持。酶产品复合物。确实，这再次由理论证实，该理论已经预测了合成酶和天然酶的eta（2）-O，O结合模式。

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