Formally Copper(III)–Alkylperoxo Complexes as Models of Possible Intermediates in Monooxygenase Enzymes

• Published in: Journal of the American Chemical Society 2017-08, Vol.139 (30), p.10220-10223
• Main Authors: Neisen, Benjamin D, Gagnon, Nicole L, Dhar, Debanjan, Spaeth, Andrew D, Tolman, William B
• Format: Article
• Language: English
• Subjects: Coordination Complexes - chemical synthesis; Coordination Complexes - chemistry; Coordination Complexes - metabolism; Copper - chemistry; Copper - metabolism; Crystallography, X-Ray; Mixed Function Oxygenases - chemistry; Mixed Function Oxygenases - metabolism; Models, Molecular; Peroxides - chemistry; Peroxides - metabolism
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/jacs.7b05754

Reaction of [NBu4]­[LCuIIOH] with excess ROOH (R = cumyl or tBu) yielded [NBu4]­[LCuIIOOR], the reversible one-electron oxidation of which generated novel species with [CuOOR]2+ cores (formally CuIIIOOR), identified by spectroscopy and theory for the case R = cumyl. This species reacts with weak O–H bonds in TEMPO-H and 4-dimethyl­aminophenol (NMe2PhOH), the latter yielding LCu­(OPhNMe2), which was also prepared independently. With the identification of [CuOOR]2+ complexes, the first precedent for this core in enzymes is provided, with implications for copper monooxygenase mechanisms.