中山大学苏成勇团队报道了通过阳离子笼在溶液中创建动态纳米空间，作为超越酶模拟的非常规C(sp)-H活化的多角色催化平台。相关研究成果发表在2021年11月15日出版的《德国应用化学》。

人工合成宿主的超分子催化最初是受酶固有反应性的生物启发，但更多的特殊性质和功能可能会超越酶模拟。

该文中，研究人员发现，基于[Pd6(RuL3)8]28+的高电荷正配位笼在溶液中创建动态纳米空间，借助仿生笼效应，多角色和多途径笼约束催化可实现多功能和异常反应性。高阳离子主体电荷驱动蛋白质中笼状球形咪唑残留物上24个咪唑NHs的部分脱质子，在溶液中产生两性不均一性，以增强针对溶液酸度的有效空穴性。

笼状疏水性、主客体静电相互作用和咪唑-N配位产生的协同作用促进了末端炔烃的C(sp)-H活化和碳阴离子中间稳定，从而在酸性条件下实现不同寻常的H/D交换和Glaser偶联，实现了水不溶性底物/产物/共催化剂的相转移，使非混溶相和双相催化成为可能，从而提供了一种有用的催化协议，将均相、非均相、酶催化和相转移催化的优点结合起来。

附：英文原文

Title: Creating Dynamic Nanospaces in Solution by Cationic Cages as Multirole Catalytic Platform for Unconventional C(sp)-H Activation Beyond Enzyme Mimics

Author: Kang Li, Kai Wu, Yu-Lin Lu, Jing Guo, Peng Hu, Cheng-Yong Su

Issue&Volume: 2021-11-15

Abstract: Supramolecular catalysis of artificial synthetic-hosts is originally bio-inspired for reactivities intrinsic to enzymes, but more exceptional properties and functions may be expected beyond enzyme mimics. Herein we demonstrate that, based on the creation of dynamic nanospaces in solution by highly charged positive coordination cage of [Pd  6  (RuL  3  )  8  ]  28+  , multirole and multi-way cageconfined catalysis is accomplishable for versatile functions and anomalous reactivities with the aid of biomimetic cage effect. The high cationic-host charges drive partial deprotonation of 24 imidazole-NHs on cage sphere alike imidazole-residuals in proteins, generating amphoteric heterogeneity in solution to enforce effective cavitybasicity against solution-acidity. Synergistic actions arisen from cage hydrophobicity, host-guest electrostatic interactions and imidazole-N coordination facilitate C(sp)-H activation and carbanionic intermediate stabilization of terminal alkynes to achieve unusual H/D-exchange and Glaser coupling under acidic conditions, and enable phase transfers of water-insoluble substrates/products/co-catalysts to make immiscible-phase and bi-phase catalysis feasible, thus providing a useful catalytic protocol to combine merits from homogeneous, heterogeneous, enzymatic and phase transfer catalysis.

DOI: 10.1002/anie.202114070

Source: https://onlinelibrary.wiley.com/doi/10.1002/anie.202114070