A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein
A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein
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DOI：
10.1021/acscatal.5b01792
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发表时间：
2015-12-01
期刊：
影响因子：
12.9
通讯作者：
Okuda, Jun
中科院分区：
文献类型：
--
作者：
Sauer, Daniel F.;Himiyama, Tomoki;Okuda, Jun
在NHC配体的主链上含有马来酰亚胺基团的一系列GRubbs-Hoveyda型催化剂前体被共价结合到β-桶蛋白Nitrobindin的空腔中。通过选择两种不同空腔大小的蛋白质突变体，并选择合适的间隔基长度，获得了一种在没有任何有机共溶剂的情况下在水中催化烯烃歧化反应的人工金属酶。在相对温和的条件下(pH 6，T=25-40℃)，4，4-二(羟甲基)-1，6-庚二烯在水中的开环歧化反应(RCM)的效率可达TON>；9000和TON>；100。
A series of Grubbs-Hoveyda type catalyst precursors for olefin metathesis containing a maleimide moiety in the backbone of the NHC ligand was covalently incorporated in the cavity of the beta-barrel protein nitrobindin. By using two protein mutants with different cavity sizes and choosing the suitable spacer length, an artificial metalloenzyme for olefin metathesis reactions in water in the absence of any organic cosolvents was obtained. High efficiencies reaching TON > 9000 in the ROMP of a water-soluble 7-oxanorbornene derivative and TON > 100 in ring-closing metathesis (RCM) of 4,4-bis(hydroxymethyl)-1,6-heptadiene in water under relatively mild conditions (pH 6, T = 25-40 degrees C) were observed.