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

doi:10.1021/jacs.7b05754

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

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

54 Scopus citations

Abstract

Reaction of [NBu₄][LCu^IIOH] with excess ROOH (R = cumyl or tBu) yielded [NBu₄][LCu^IIOOR], the reversible one-electron oxidation of which generated novel species with [CuOOR]²⁺ cores (formally Cu^IIIOOR), 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(OPh^NMe2), 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 language	English (US)
Pages (from-to)	10220-10223
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	139
Issue number	30
DOIs	https://doi.org/10.1021/jacs.7b05754
State	Published - Aug 2 2017

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© 2017 American Chemical Society.

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10.1021/jacs.7b05754

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6132249

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title = "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.",

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T1 - Formally Copper(III)-Alkylperoxo Complexes as Models of Possible Intermediates in Monooxygenase Enzymes

AU - Neisen, Benjamin D.

AU - Gagnon, Nicole L.

AU - Dhar, Debanjan

AU - Spaeth, Andrew D

AU - Tolman, William B

PY - 2017/8/2

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N2 - 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.

AB - 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.

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

Abstract

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