Lipase active site covalent anchoring of Rh(NHC) catalysts: Towards chemoselective artificial metalloenzymes
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Publication date
2015-04-21
Authors
Basauri Molina, Manuel
Riemersma, C. F.
Würdemann, M. A.
Kleijn, H.
Klein Gebbink, R.J.M.
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Article
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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
Keywords
General Chemistry, Catalysis, Ceramics and Composites, Electronic, Optical and Magnetic Materials, Surfaces, Coatings and Films, Materials Chemistry, Metals and Alloys
Citation
Basauri-Molina, M, Riemersma, C F, Würdemann, M A, Kleijn, H & Klein Gebbink, R J M 2015, 'Lipase active site covalent anchoring of Rh(NHC) catalysts : Towards chemoselective artificial metalloenzymes', Chemical Communications, vol. 51, no. 31, pp. 6792-6795. https://doi.org/10.1039/c4cc09700a