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

Chemical Communications : Chem Comm
M Basauri-MolinaR J M Klein Gebbink

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.

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Citations

Mar 13, 2020·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Katsunori Tanaka, Kenward Vong
Jul 22, 2020·Chemical Communications : Chem Comm·Woo Jae JeongWoon Ju Song
Jul 17, 2015·Angewandte Chemie·Leo E HeimMartin H G Prechtl
Sep 9, 2015·Chemistry : a European Journal·Manuel Basauri-MolinaRobertus J M Klein Gebbink
Dec 7, 2018·Chemical Society Reviews·Yanlan WangAlaa S Abd-El-Aziz
Jun 17, 2020·Chemistry : a European Journal·Matteo PlanchestainerMartin Albrecht
Jul 18, 2017·Chemical Reviews·Fabian SchwizerThomas R Ward

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