Heme oxygenase, steering dioxygen activation toward heme hydroxylation.
Heme oxygenase, steering dioxygen activation toward heme hydroxylation.
复制标题
血红素加氧酶，将双氧激活转向血红素羟基化。
DOI：
10.1016/j.jinorgbio.2004.09.016
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发表时间：
2005
影响因子：
3.9
通讯作者：
Zeng,Yuhong
中科院分区：
文献类型：
--
作者：
Rivera,Mario;Zeng,Yuhong
血红素加氧酶对双氧的激活是通过形成必需的氢过氧化铁中间体 (FeIII-OOH) 进行的，就像单加氧酶对双氧的激活一样。这篇综述总结了目前对血红素加氧酶的结构和动态特性的理解，这些特性将 FeIII-OOH 中间体的反应性引导至血红素羟基化而不是氧铁基形成。此外，在最近的 X 射线和核磁共振光谱研究的背景下，对决定血红素氧合区域特异性的结构和电子因素进行了分析。还讨论了血红素加氧酶进行的血红素羟基化和耦合氧化过程之间机制的差异。
The activation of dioxygen by heme oxygenase proceeds via formation of an obligatory ferric hydroperoxide intermediate (FeIII–OOH), as is the case in the activation of dioxygen by monooxygenase enzymes. This review summarizes current understanding of the structural and dynamic properties in heme oxygenase that channel the reactivity of the FeIII-OOH intermediate toward heme hydroxylation rather than oxoferryl formation. In addition, structural and electronic factors dictating the regiospecificity of heme oxygenation are analyzed in the context of recent X-ray and NMR spectroscopic studies. Differences in mechanism between heme hydroxylation, as carried out by heme oxygenase, and the coupled oxidation process, are also addressed.