Coordination Dynamics of Iron is a Key Player in the Catalysis of Non-heme Enzymes |
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| Authors: | Jinyan Zhang Dr Peng Wu Dr Xuan Zhang Prof Binju Wang |
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| Affiliation: | 1. 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;2. State Key Laboratory of High-Efficiency Utilization of Coal and, Green Chemical Engineering, School of Chemistry and Chemical Engineering, Ningxia University, Yinchuan, 750021 China;3. Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211 China |
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| Abstract: | 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. |
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| Keywords: | coordination dynamics C−N coupling C−O coupling C−S coupling non-heme enzymes selectivity |
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