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

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.

SUBMITTER: Neisen BD 

PROVIDER: S-EPMC6132249 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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

Neisen Benjamin D BD   Gagnon Nicole L NL   Dhar Debanjan D   Spaeth Andrew D AD   Tolman William B WB  

Journal of the American Chemical Society 20170719 30

Reaction of [NBu<sub>4</sub>][LCu<sup>II</sup>OH] with excess ROOH (R = cumyl or tBu) yielded [NBu<sub>4</sub>][LCu<sup>II</sup>OOR], the reversible one-electron oxidation of which generated novel species with [CuOOR]<sup>2+</sup> cores (formally Cu<sup>III</sup>OOR), identified by spectroscopy and theory for the case R = cumyl. This species reacts with weak O-H bonds in TEMPO-H and 4-dimethylaminophenol (<sup>NMe2</sup>PhOH), the latter yielding LCu(OPh<sup>NMe2</sup>), which was also prepared  ...[more]

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