Nitrene Transfer Catalyzed by a Non-Heme Iron Enzyme and Enhanced by Non-Native Small-Molecule Ligands

• Published in: Journal of the American Chemical Society Vol. 141; no. 50; pp. 19585 - 19588
• Main Authors: Goldberg, Nathaniel W, Knight, Anders M, Zhang, Ruijie K, Arnold, Frances H
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 18-12-2019
• Subjects: Alkenes - chemistry; Aziridines - chemistry; Biocatalysis; Directed Molecular Evolution; Ligands; Models, Molecular; Nonheme Iron Proteins - chemistry; Nonheme Iron Proteins - genetics; Nonheme Iron Proteins - metabolism; Protein Conformation; Pseudomonas - enzymology
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/jacs.9b11608

Transition-metal catalysis is a powerful tool for the construction of chemical bonds. Here we show that Pseudomonas savastanoi ethylene-forming enzyme, a non-heme iron enzyme, can catalyze olefin aziridination and nitrene C–H insertion, and that these activities can be improved by directed evolution. The non-heme iron center allows for facile modification of the primary coordination sphere by addition of metal-coordinating molecules, enabling control over enzyme activity and selectivity using small molecules.