Catalytic Phenol Hydroxylation with Dioxygen: Extension of the Tyrosinase Mechanism beyond the Protein Matrix1. Issue 20 (22nd April 2013)

• Record Type: Journal Article
• Authors: Hoffmann, Alexander; Citek, Cooper; Binder, Stephan; Goos, Arne; Rübhausen, Michael; Troeppner, Oliver; Ivanović‐Burmazović, Ivana; Wasinger, Erik C.; Stack, T. Daniel P.; Herres‐Pawlis, Sonja
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 20(2013)
• Page Start: 5398
• Page End: 5401
• Publication Date: 2013-04-22
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201301249
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>A new catalyst</bold> (see structure) hydroxylates phenols with O₂ 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 NEt₃ and even non‐native substrates can be oxidized catalytically. The reaction mechanism is analogous to that of the enzyme‐catalyzed reaction.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1zsxhx1b" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>