中文摘要：

金属酶催化的高效性和选择性来源于第一配位环境金属催化中心和第二配位环境非共价相互作用力的协同作用。针对金属催化中心构效关系的研究已有大量报道，相比之下，有关非共价相互作用的研究尚不够充分。金属酶的非共价作用力，包括氢键、静电相互作用、范德华力和疏水相互作用等产生于第二配位环境中的氨基酸残基。阐述第二配位环境中氨基酸残基作用的首要障碍来自于复杂并难以界定的分子内和分子间的相互作用网络。制备包含非共价相互作用的金属酶模拟物是攻克这一难题行之有效的方法，它不但有利于理解非共价相互作用和金属离子之间的协同作用，而且有助于发展可应用于工业、医药、生物技术等领域的仿生催化剂。本文按照非共价弱相互作用的类型，对近期报道的典型案例进行综述。文中阐述了基于简单多齿配体，如联吡啶、三联吡啶、环胺、卟啉等，和基于超分子配体，如功能化的环糊精和杯芳烃等的金属酶模型物。在讨论模型物之前，本文对天然金属酶中的非共价相互作用简略探讨。

英文摘要：

Metalloenzyme efficiency and specificity originate from the cooperative roles between the metalmediated catalysis at the first coordination sphere and the non-covalent interactions at the secondary coordination sphere. While the structures and functions of metal coordination sites have drawn wide researches, the elucidations of the non-covalent interactions have been less assessed. The enzymatic non-covalent interactions in terms of hydrogen bonding, electrostatic attraction, van der Waals force and hydrophobic interaction are produced from the amino acid residues in the secondary coordination sphere. The primary hurdle that hampers the elucidation of the amino acids in the secondary coordination sphere is their complicated intra- and intermolecular interaction networks that are exceptionally difficult to define. A practical approach to circumvent this challenge is to prepare metalloenzyme mimics that include non-covalent interactions. This approach not only opens an avenue to understand the synergism between the non-covalent interactions and the metal ions, but also contributes to the development of biomimetic catalysts applied in industry, pharmaceutics, biotechnology and even wider areas. To make an overview of the recent progresses in this field, this review discusses the representative mimics which are organized according to the interaction categories. The mimics exemplified here include the ones based on the simple multi-dentate ligands like bipyridine, terpyridine, cyclic amine and porphyrin, and the supramolecular ligands like thefunctionalized cyclodextrins and calixarenes. Prior to the discussions of mimics, the non-covalent interactions of native metalloenzymes are commented.