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Issue 7, 2015
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Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism

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Abstract

A new tridentate N-donor ligand and its corresponding copper(I) complex have been synthesized to investigate the tyrosinase-like aromatic hydroxylation of an attached phenol. The results of the oxygenation reactions are compared to related systems having attached phenyl and catechol groups, respectively. The title complex is the first system mediating the monooxygenation of a phenol in the absence of an external base.

Graphical abstract: Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism

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Article information


Submitted
30 Sep 2014
Accepted
28 Dec 2014
First published
05 Jan 2015

Dalton Trans., 2015,44, 3251-3258
Article type
Paper

Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism

J. N. Hamann, M. Rolff and F. Tuczek, Dalton Trans., 2015, 44, 3251
DOI: 10.1039/C4DT03010A

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