An iron nitride complex
An iron nitride complex
复制标题
DOI：
10.1002/anie.200800600
复制
发表时间：
2008-01-01
影响因子：
16.6
通讯作者：
Meyer, Karsten
中科院分区：
文献类型：
--
作者：
Vogel, Carola;Heinemann, Frank W.;Meyer, Karsten
高氧化态铁的配位化合物已被用作生物催化中的反应中间体。铁（IV）铁酰基物质是这种高度反应性物质的实例，其长期以来已知位于加氧酶的催化中心。[1]通过对固氮酶的X射线衍射研究，最近有人提出氮化铁部分存在于生物氮还原的位点。[2]因此，良好的特征高价铁配合物已被寻求作为含铁酶介导的转化的仿生模型。为了了解氮化铁的反应性和这些物种在生物催化中的可能作用，深入了解稳定[FeN]合成子的络合物的分子结构是非常必要的。虽然在Fe= NR和Fe N物种的合成和光谱解析方面取得了重大进展，[3-6]但尚未完成具有末端Fe N官能度的络合物的X射线晶体学表征。[7，8]第一个晶体学表征的单核FeIV= O实体在由大环四-N-甲基化cyclam配体提供的八面体环境中稳定。[9]类似的cyclam衍生物也允许八面体的FeV和FeVI氮化物复合物在异常高的氧化中的稳定和详细的光谱表征
Coordination compounds of iron in high oxidation states have been invoked as reactive intermediates in biocatalyses. Iron (IV) ferryl species are examples of such highly reactive species that have long been known to be at the catalytic centers of oxygenases.[1] Supported by X-ray diffraction studies on nitrogenase, the iron nitride moiety has recently been suggested to be present at the site of biological nitrogen reduction.[2] As a result, well-characterized high-valent iron complexes have been sought as biomimetic models for transformations mediated by iron-containing enzymes. To gain understanding of iron nitride reactivity and the possible role of such species in biocatalysis, insight into the molecular structure of complexes stabilizing the [FeN] synthon is highly desirable. Whereas significant progress has been made in the synthesis and spectroscopic elucidation of Fe= NR and Fe N species,[3–6] X-ray crystallographic characterization of a complex with a terminal Fe N functionality has not been accomplished.[7, 8]The first mononuclear FeIV= O entity crystallographically characterized was stabilized in an octahedral environment provided by a macrocyclic tetra-N-methylated cyclam ligand.[9] Similar cyclam derivatives also allow the stabilization and detailed spectroscopic characterization of octahedral FeV and FeVI nitride complexes in unusually high oxidation