Catalytic phenol hydroxylation with dioxygen: Extension of the tyrosinase mechanism beyond the protein matrix

Hoffmann A, Citek C, Binder S, Goos A, Rübhausen M, Tröppner O, Ivanovic-Burmazovic I, Wasinger EW, Stack TDP, Herres-Pawlis S (2013)


Publication Type: Journal article, Original article

Publication year: 2013

Journal

Original Authors: Hoffmann A., Citek C., Binder S., Goos A., Rübhausen M., Troeppner O., Ivanovic̈-Burmazovic̈ I., Wasinger E., Stack T., Herres-Pawlis S.

Publisher: Wiley-VCH Verlag

Book Volume: 52

Pages Range: 5398-5401

Journal Issue: 20

DOI: 10.1002/anie.201301249

Abstract

A new catalyst (see structure) hydroxylates phenols with O via a stable side-on peroxide complex, which is similar to the active site of tyrosinase in terms of the ligand environment and its spectroscopic properties. The catalytic oxidation of phenols to quinones proceeds at room temperature in the presence of NEt and even non-native substrates can be oxidized catalytically. The reaction mechanism is analogous to that of the enzyme-catalyzed reaction. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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How to cite

APA:

Hoffmann, A., Citek, C., Binder, S., Goos, A., Rübhausen, M., Tröppner, O.,... Herres-Pawlis, S. (2013). Catalytic phenol hydroxylation with dioxygen: Extension of the tyrosinase mechanism beyond the protein matrix. Angewandte Chemie International Edition, 52(20), 5398-5401. https://dx.doi.org/10.1002/anie.201301249

MLA:

Hoffmann, Alexander, et al. "Catalytic phenol hydroxylation with dioxygen: Extension of the tyrosinase mechanism beyond the protein matrix." Angewandte Chemie International Edition 52.20 (2013): 5398-5401.

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