Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes
Lipase active site covalent anchoring of Rh(NHC) catalysts: towards chemoselective artificial metalloenzymes
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DOI：
10.1039/c4cc09700a
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发表时间：
2015-01-01
影响因子：
4.9
通讯作者：
Gebbink, R. J. M. Klein
中科院分区：
文献类型：
--
作者：
Basauri-Molina, M.;Riemersma, C. F.;Gebbink, R. J. M. Klein
Rh（NHC）膦酸盐络合物与脂肪酶角质酶和南极假丝酵母脂肪酶B反应，导致通过共价活性定点杂交形成第一种（可溶性）人工金属酶。当与无支撑的复合物相比时，这些新的稳健的混合物在烯烃对酮的（竞争性）氢化中显示出增强的化学选择性。
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.