Title : Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes - Basauri-Molina_2015_Chem.Commun.(Camb)_51_6792 |
Author(s) : Basauri-Molina M , Riemersma CF , Wurdemann MA , Kleijn H , Klein Gebbink RJ |
Ref : Chem Commun (Camb) , 51 :6792 , 2015 |
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. |
PubMedSearch : Basauri-Molina_2015_Chem.Commun.(Camb)_51_6792 |
PubMedID: 25786894 |
Gene_locus related to this paper: canar-LipB , fusso-cutas |
Inhibitor | Rh-pNP |
Gene_locus | canar-LipB fusso-cutas |
Basauri-Molina M, Riemersma CF, Wurdemann MA, Kleijn H, Klein Gebbink RJ (2015)
Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes
Chem Commun (Camb)
51 :6792
Basauri-Molina M, Riemersma CF, Wurdemann MA, Kleijn H, Klein Gebbink RJ (2015)
Chem Commun (Camb)
51 :6792