Probing the mechanism of O2 activation by a copper(I) biomimetic complex of a C-H hydroxylating copper monooxygenase

Albert Poater*, Luigi Cavallo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

In this paper, we report, for the first time, a plausible full reaction pathway for the activation of O2 by a tetraazamacrocyclic monocopper(I) complex and for the subsequent intramolecular alkylic hydroxylation to yield the alkoxide product. This theoretical insight offers remarkable support to the fundamental hypothesis in the field that a hydroperoxo complex of the type CuIIOOH intermediate is the key intermediate in this class of reactions. Overall, we give insight into an intramolecular alkylic C-H bond activation due to the O2 binding to copper(I) with an end-on 1-O2 ligation. The loss of a water molecule involves the final substrate oxygenation. The complex we consider is a biomimetic of several systems of biological relevance, such as amine oxidases, peptidylglycine-a- hydroxylating monooxygenase, and dopamine-/? monooxygenases.

Original languageEnglish (US)
Pages (from-to)4062-4066
Number of pages5
JournalInorganic Chemistry
Volume48
Issue number9
DOIs
StatePublished - May 4 2009

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

Fingerprint Dive into the research topics of 'Probing the mechanism of O2 activation by a copper(I) biomimetic complex of a C-H hydroxylating copper monooxygenase'. Together they form a unique fingerprint.

Cite this