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

M. Basauri-Molina; C. F. Riemersma; M. A. Würdemann; H. Kleijn; R. J M Klein Gebbink

doi:10.1039/c4cc09700a

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

M. Basauri-Molina, C. F. Riemersma, M. A. Würdemann, H. Kleijn, R. J M Klein Gebbink^*

^*Corresponding author for this work

Sub Organic Chemistry and Catalysis

Utrecht University

Research output: Contribution to journal › Article › Academic › peer-review

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. This journal is

Original language	English
Pages (from-to)	6792-6795
Number of pages	4
Journal	Chemical Communications
Volume	51
Issue number	31
DOIs	https://doi.org/10.1039/c4cc09700a
Publication status	Published - 21 Apr 2015

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AU - Kleijn, H.

AU - Klein Gebbink, R. J M

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

Abstract

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