title: 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.
authors: Organic Chemistry and Catalysis, Debye Institute for Nanomaterials Science, Utrecht University, Universiteitsweg 99, 3584CG Utrecht, The Netherlands. r.j.m.kleingebbink@uu.nl.
authors: M
authors: M
authors: Basauri-Molina
authors: C F
authors: CF
authors: Riemersma
authors: M A
authors: MA
authors: Würdemann
authors: H
authors: H
authors: Kleijn
authors: R J M
authors: RJ
authors: Klein Gebbink
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D002384:Catalysis; D020134:Catalytic Domain; D005656:Fungal Proteins / Q000737:chemistry*; D006571:Heterocyclic Compounds / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D008697:Methane / Q000031:analogs & derivatives* / Q000737:chemistry; D009942:Organometallic Compounds / Q000737:chemistry*; D012238:Rhodium / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; D006571:Heterocyclic Compounds; D009942:Organometallic Compounds; C030011:carbene; D012238:Rhodium; D008049:Lipase; C431349:lipase B, Candida antarctica; D008697:Methane