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O-2 Activation by Non-Heme Iron Enzymes

机译：非血红素铁酶激活O-2

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The non-heme Fe enzymes are ubiquitous in nature and perform a wide range of functions involving O-2 activation. These had been difficult to study relative to heme enzymes; however, spectroscopic methods that provide significant insight into the correlation of structure with function have now been developed. This Current Topics article summarizes both the molecular mechanism these enzymes use to control O-2 activation in the presence of cosubstrates and the oxygen intermediates these reactions generate. Three types of O-2 activation are observed. First, non-heme reactivity is shown to be different from heme chemistry where a low-spin Fe-III-OOH non-heme intermediate directly reacts with substrate. Also, two subclasses of non-herne Fe enzymes generate high-spin Fe-IV=O intermediates that provide both sigma and pi frontier molecular orbitals that can control selectivity. Finally, for several subclasses of non-herne Fe enzymes, binding of the substrate to the Fe-II site leads to the one-electron reductive activation of O-2 to an Fe-III-superoxide capable of H atom abstraction and electrophilic attack.
机译：非血红素铁酶在自然界中普遍存在，并执行涉及O-2活化的多种功能。相对于血红素酶，这些很难研究。但是，现在已经开发出了可以显着了解结构与功能之间关系的光谱方法。这篇当前主题文章总结了在共底物存在下这些酶用于控制O-2活化的分子机制，以及这些反应产生的氧中间体。观察到三种类型的O-2活化。首先，非血红素的反应性显示出与血红素化学不同，后者的低自旋Fe-III-OOH非血红素中间体与底物直接反应。同样，非黑素铁酶的两个亚类产生高自旋的Fe-IV = O中间体，它们提供可控制选择性的σ和pi前沿分子轨道。最后，对于非亚铁Fe酶的几种亚类，底物与Fe-II位点的结合导致O-2的单电子还原活化为能够进行H原子抽象和亲电攻击的Fe-III超氧化物。

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