Li Rui-Ning, Chen Shi-Lu
Key Laboratory of Cluster Science of Ministry of Education, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing, 100081, China.
Chembiochem. 2025 Feb 1;26(3):e202400788. doi: 10.1002/cbic.202400788. Epub 2024 Nov 25.
Oxoiron(IV) complexes are key intermediates in the catalytic reactions of some non-heme diiron enzymes. These enzymes, across various subfamilies, activate dioxygen to generate high-valent diiron-oxo species, which, in turn, drive the activation of substrates and mediate a variety of challenging oxidative transformations. In this review, we summarize the structures, formation mechanisms, and functions of high-valent diiron-oxo intermediates in eight representative diiron enzymes (sMMO, RNR, ToMO, MIOX, PhnZ, SCD1, AlkB, and SznF) spanning five subfamilies. We also categorize and analyze the structural and mechanistic differences among these enzymes.
氧代铁（IV）配合物是一些非血红素双铁酶催化反应中的关键中间体。这些酶分布于各个亚家族，可激活双氧以生成高价双铁-氧物种，进而驱动底物的活化并介导各种具有挑战性的氧化转化反应。在本综述中，我们总结了来自五个亚家族的八种代表性双铁酶（可溶性甲烷单加氧酶、核糖核苷酸还原酶、甲苯单加氧酶、肌醇氧化酶、菲啶还原酶、硬脂酰辅酶A去饱和酶1、AlkB和SznF）中高价双铁-氧中间体的结构、形成机制及功能。我们还对这些酶之间的结构和机制差异进行了分类和分析。
