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

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 chemoselecti...

Full description

Bibliographic Details
Main Authors: Basauri-Molina, M., Riemersma, C. F., Würdemann, M. A., Kleijn, H., Klein Gebbink, R. J M
Other Authors: Organic Chemistry and Catalysis, Sub Organic Chemistry and Catalysis
Format: Article in Journal/Newspaper
Language:English
Published: 2015
Subjects:
Chemistry(all)
Catalysis
Ceramics and Composites
Electronic
Optical and Magnetic Materials
Surfaces
Coatings and Films
Materials Chemistry
Metals and Alloys
Antarc*
Antarctica
Online Access:https://dspace.library.uu.nl/handle/1874/427933
Description
Summary: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

Similar Items