Dipartimento di Scienze Farmaceutiche, Università degli Studi di Milano, Via Venezian 21, 20133 Milano, Italy.
Scuola Normale Superiore, Piazza dei Cavalieri 7, 56126 Pisa, Italy.
Inorg Chem. 2021 Mar 1;60(5):2976-2982. doi: 10.1021/acs.inorgchem.0c02969. Epub 2021 Feb 8.
Based on the supramolecular interaction between vancomycin (Van), an antibiotic glycopeptide, and D-Ala-D-Ala (DADA) dipeptides, a novel class of artificial metalloenzymes was synthesized and characterized. The presence of an iridium(III) ligand at the -terminus of DADA allowed the use of the metalloenzyme as a catalyst in the asymmetric transfer hydrogenation of cyclic imines. In particular, the type of link between DADA and the metal-chelating moiety was found to be fundamental for inducing asymmetry in the reaction outcome, as highlighted by both computational studies and catalytic results. Using the [IrCp*()Cl]Cl ⊂ Van complex in 0.1 M CHCOONa buffer at pH 5, a significant 70% () e.e. was obtained in the reduction of quinaldine .
基于抗生素糖肽万古霉素（Van）与 D-Ala-D-Ala（DADA）二肽之间的超分子相互作用，合成并表征了一类新型人工金属酶。DADA 的 -末端存在铱（III）配体，这使得金属酶可以作为环状亚胺不对称转移氢化反应的催化剂。特别是，DADA 和金属螯合部分之间的连接类型被发现是诱导反应结果不对称的关键因素，这一点通过计算研究和催化结果都得到了证实。使用 [IrCp*()Cl]Cl⊂Van 配合物在 0.1 M CHCOONa 缓冲液（pH 5）中，在喹哪啶的还原中获得了显著的 70%（）对映体过量值。
