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

Benjamin D. Neisen, Nicole L. Gagnon, Debanjan Dhar, Andrew D Spaeth, William B Tolman

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)10220-10223
Number of pages4
JournalJournal of the American Chemical Society
Volume139
Issue number30
DOIs
StatePublished - Aug 2 2017

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