2023 article

Repurposing Iron- and 2-Oxoglutarate-Dependent Oxygenases to Catalyze Olefin Hydration

Wang, B., Lu, Y., Cha, L., Chen, T.-Y., Palacios, P. M., Li, L., … Chen, C. (2023, September 6). ANGEWANDTE CHEMIE-INTERNATIONAL EDITION.

By: B. Wang *, Y. Lu *, L. Cha n , T. Chen n, P. Palacios*, L. Li *, Y. Guo *, W. Chang n , C. Chen *

author keywords: Biocatalysis; Hydrogen Atom Transfer; Mukaiyama Hydration; Nonheme Fe/2OG-Dependent Oxygenase
TL;DR: It is shown that various enzymes of this family, when reconstituted with Fe(II) or Fe(III), can catalyze Mukaiyama hydration-a redox neutral transformation and demonstrates that Fe/2OG enzymes have utility in catalysis beyond the current scope of catalytic oxidation. (via Semantic Scholar)
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Source: Web Of Science
Added: September 11, 2023

AbstractMononuclear nonheme iron(II) and 2‐oxoglutarate (Fe/2OG)‐dependent oxygenases and halogenases are known to catalyze a diverse set of oxidative reactions, including hydroxylation, halogenation, epoxidation, and desaturation in primary metabolism and natural product maturation. However, their use in abiotic transformations has mainly been limited to C−H oxidation. Herein, we show that various enzymes of this family, when reconstituted with Fe(II) or Fe(III), can catalyze Mukaiyama hydration—a redox neutral transformation. Distinct from the native reactions of the Fe/2OG enzymes, wherein oxygen atom transfer (OAT) catalyzed by an iron‐oxo species is involved, this nonnative transformation proceeds through a hydrogen atom transfer (HAT) pathway in a 2OG‐independent manner. Additionally, in contrast to conventional inorganic catalysts, wherein a dinuclear iron species is responsible for HAT, the Fe/2OG enzymes exploit a mononuclear iron center to support this reaction. Collectively, our work demonstrates that Fe/2OG enzymes have utility in catalysis beyond the current scope of catalytic oxidation.