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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >How do the thiolate ligand and its relative position control the oxygen activation in the cysteine dioxygenase model?
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How do the thiolate ligand and its relative position control the oxygen activation in the cysteine dioxygenase model?

机译：硫醇盐配体及其相对位置如何控制半胱氨酸双加氧酶模型中的氧活化？

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摘要

In the iron(II)-thiolate models of cysteine dioxygenase, the thiolate ligand is a key factor in the oxygen activation. In this contribution, four model compounds have been theoretically investigated. This comparative study reveals that the thiolate ligand itself and its relative position are both important for the activation of O _2. Before the O _2 binding, the thiolate ligand must transfer charge to Fe(II), and the effective nuclear charges of Fe(II) is decreased, which results in a lower redox potential of compounds. In other words, the thiolate ligand provides a prerequisite for the O _2 activation. Furthermore, the relative position of the thiolate ligand is discovered to determine the reaction path of O _2 activation. The amount of charge transfer is crucial for these reactions; the more charge it transfers, the lower the related redox potentials. This work really helps think deeper into the O _2 activation process of mononuclear nonheme iron enzymes.
机译：在半胱氨酸双加氧酶的铁（II）-硫醇盐模型中，硫醇盐配体是氧活化的关键因素。在此贡献中，理论上对四种模型化合物进行了研究。这项比较研究表明，硫醇盐配体本身及其相对位置对于O _2的活化都很重要。在O _2结合之前，硫醇盐配体必须将电荷转移到Fe（II），并且Fe（II）的有效核电荷降低，从而导致化合物的氧化还原电位降低。换句话说，硫醇盐配体为O _2活化提供了先决条件。此外，发现硫醇盐配体的相对位置决定了O _2活化的反应路径。电荷转移的数量对于这些反应至关重要。转移的电荷越多，相关的氧化还原电势就越低。这项工作确实有助于更深入地思考单核非血红素铁酶的O _2活化过程。

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