Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 27, 2016
Previous Article Next Article

Supramolecular control of monooxygenase reactivity in a copper(ii) cryptate

Author affiliations

Abstract

We report a detailed investigation of the formation and self-decomposition of Cu(II)–hydroperoxo intermediates under the influence of second-coordination-sphere features provided by a cryptand. In solution, an equilibrium between two copper complexes with square-planar and square-pyramidal geometries was identified. Upon addition of H2O2/Et3N, two copper(II)–hydroperoxo intermediates formed at different rates. Their decomposition via self-oxidation was probed by deuterating select positions on the cryptand. This led to a small kinetic isotope effect of 1.5. Mass spectrometry analysis of the demetallated organic products is consistent with a direct oxygen-atom transfer to a tertiary amine on the cryptand, forming an N-oxide, unlike other models of copper mononuclear monooxygenase enzymes.

Graphical abstract: Supramolecular control of monooxygenase reactivity in a copper(ii) cryptate

Back to tab navigation

Supplementary files

Article information


Submitted
03 Feb 2016
Accepted
13 Jun 2016
First published
13 Jun 2016

Dalton Trans., 2016,45, 11109-11119
Article type
Paper
Author version available

Supramolecular control of monooxygenase reactivity in a copper(II) cryptate

L. Chaloner, A. Khomutovskaya, F. Thomas and X. Ottenwaelder, Dalton Trans., 2016, 45, 11109
DOI: 10.1039/C6DT00490C

Social activity

Search articles by author

Spotlight

Advertisements