Crystallographic and spectroscopic characterization of a nonheme Fe(IV)=O complex
Crystallographic and spectroscopic characterization of a nonheme Fe(IV)=O complex
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DOI：
10.1126/science.299.5609.1037
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发表时间：
2003-02-14
期刊：
影响因子：
56.9
通讯作者：
Que, L
中科院分区：
文献类型：
--
作者：
Rohde, JU;In, JH;Que, L
根据血红素范式，人们经常提出，非血红素单铁酶对氧气的激活涉及负责底物氧化步骤的铁(IV)=氧中间体。这种暂态物种现在已经从一个带有非血红素大环配体的合成络合物中获得，并用光谱进行了表征。它的高分辨晶体结构揭示了铁-氧键的长度为1.646(3)埃，这表明在非卟啉配体环境中可以存在末端的铁(IV)=氧单元，从而终止了对非血红素铁催化机理的看法。
Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and [ending credence to proposed mechanisms of nonheme iron catalysis.