State Key Laboratory of Physical Chemistry of Solid Surfaces and, Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
State Key Laboratory of High-Efficiency Utilization of Coal and, Green Chemical Engineering, School of Chemistry and Chemical Engineering, Ningxia University, Yinchuan, 750021, China.
Chembiochem. 2023 Jul 17;24(14):e202300119. doi: 10.1002/cbic.202300119. Epub 2023 Jun 20.
Mononuclear nonheme iron enzymes catalyze a large variety of oxidative transformations responsible for various biosynthesis and metabolism processes. Unlike their P450 counterparts, non-heme enzymes generally possess flexible and variable coordination architecture, which can endow rich reactivity for non-heme enzymes. This Concept highlights that the coordination dynamics of iron can be a key player in controlling the activity and selectivity of non-heme enzymes. In ergothioneine synthase EgtB, the coordination switch of the sulfoxide radical species enables the efficient and selective C-S coupling reaction. In iron(II)- and 2-oxoglutarate-dependent (Fe/2OG) oxygenases, the conformational flip of ferryl-oxo intermediate can be extensively involved in selective oxidation reactions. Especially, the five-coordinate ferryl-oxo species may allow the substrate coordination via O or N atom, which may facilitate the C-O or C-N coupling reactions via stabilizing the transition states and inhibiting the unwanted hydroxylation reactions.
单核非血红素铁酶催化多种氧化转化反应，这些反应负责各种生物合成和代谢过程。与细胞色素 P450 酶不同，非血红素酶通常具有灵活多变的配位结构，这赋予了非血红素酶丰富的反应性。本综述强调了铁的配位动力学可以成为控制非血红素酶活性和选择性的关键因素。在麦硫因合酶 EgtB 中，亚砜自由基物种的配位开关能够实现高效且选择性的 C-S 偶联反应。在铁(II)和 2-氧戊二酸依赖性（Fe/2OG）加氧酶中，过氧铁-氧中间体的构象翻转可以广泛参与选择性氧化反应。特别是，五配位的过氧铁-氧物种可能允许通过 O 或 N 原子进行底物配位，这可能通过稳定过渡态和抑制不必要的羟基化反应来促进 C-O 或 C-N 偶联反应。
