Issue 31, 2015

Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes

Abstract

A Rh(NHC) phosphonate complex reacts with the lipases cutinase and Candida antarctica lipase B resulting in the first (soluble) artificial metalloenzymes formed by covalent active site-directed hybridization. When compared to unsupported complexes, these new robust hybrids show enhanced chemoselectivity in the (competitive) hydrogenation of olefins over ketones.

Graphical abstract: Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes

Supplementary files

Article information

Article type
Communication
Submitted
04 Dec 2014
Accepted
10 Mar 2015
First published
11 Mar 2015
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2015,51, 6792-6795

Author version available

Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes

M. Basauri-Molina, C. F. Riemersma, M. A. Würdemann, H. Kleijn and R. J. M. Klein Gebbink, Chem. Commun., 2015, 51, 6792 DOI: 10.1039/C4CC09700A

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