Issue 2, 2015

Laccases as palladium oxidases

Abstract

The first example of a coupled catalytic system involving an enzyme and a palladium(II) catalyst competent for the aerobic oxidation of alcohol in mild conditions is described. In the absence of dioxygen, the fungal laccase LAC3 is reduced by a palladium(0) species as evidenced by the UV/VIS and ESR spectra of the enzyme. During the oxidation of veratryl alcohol performed in water, at room temperature and atmospheric pressure, LAC3 regenerates the palladium catalyst, is reduced and catalyzes the four-electron reduction of dioxygen into water with no loss of enzyme activity. The association of a laccase with a water-soluble palladium complex results in a 7-fold increase in the catalytic efficiency of the complex. This is the first step in the design of a family of renewable palladium catalysts for aerobic oxidation.

Graphical abstract: Laccases as palladium oxidases

Supplementary files

Article information

Article type
Edge Article
Submitted
22 Aug 2014
Accepted
10 Nov 2014
First published
14 Nov 2014
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2015,6, 1247-1251

Author version available

Laccases as palladium oxidases

Y. Mekmouche, L. Schneider, P. Rousselot-Pailley, B. Faure, A. J. Simaan, C. Bochot, M. Réglier and T. Tron, Chem. Sci., 2015, 6, 1247 DOI: 10.1039/C4SC02564D

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