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

51 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

Bibliographical note

Publisher Copyright:
© 2017 American Chemical Society.

Access

10.1021/jacs.7b05754

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

OpenUrl availability

Full text

Cite this

@article{7411ba3b0eb14ee5aa918c1d320a0bc6,

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.",

author = "Neisen, {Benjamin D.} and Gagnon, {Nicole L.} and Debanjan Dhar and Spaeth, {Andrew D} and Tolman, {William B}",

note = "Publisher Copyright: {\textcopyright} 2017 American Chemical Society.",

year = "2017",

month = aug,

day = "2",

doi = "10.1021/jacs.7b05754",

language = "English (US)",

volume = "139",

pages = "10220--10223",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "30",

}

TY - JOUR

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

Y1 - 2017/8/2

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.

UR - http://www.scopus.com/inward/record.url?scp=85026799580&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85026799580&partnerID=8YFLogxK

U2 - 10.1021/jacs.7b05754

DO - 10.1021/jacs.7b05754

M3 - Article

C2 - 28722408

AN - SCOPUS:85026799580

SN - 0002-7863

VL - 139

SP - 10220

EP - 10223

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 30

ER -

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

Abstract

Bibliographical note

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this