Metal-Ligand Cooperative Effect on Intramolecular Electron Transfer in Macrocycle-Encircled Copper-Oxygen Species

作     者：Siqi Zhang Liang Zhao 

作者机构：Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology(Ministry of Education)Department of ChemistryTsinghua UniversityBeijing 100084 

出 版 物：《CCS Chemistry》 (中国化学会会刊（英文）)

年 卷 期：2023年第5卷第9期

页      面：2171-2183页

核心收录：

学科分类：08[工学] 080502[工学-材料学] 0805[工学-材料科学与工程（可授工学、理学学位）] 

基　　金：Financial support by NSFC(22025105,91956125,and 21821001) the Shuimu Tsinghua Scholar Program is gratefully acknowledged 

主　　题：metal-ligand cooperativity bimetallic cooperativity macrocyclic ligands copper-oxygen species intramolecular electron transfer 

摘      要：Reproduction of ubiquitous metal-ligand cooperativity in copper-oxygen enzyme mimics is crucial for the comprehension of catalytic mechanisms in coppercontaining enzymes and copper-catalyzed chemical *** we describe the synthesis and reduction behavior of a series of encapsulated dinuclear copper-oxygen species by systematically altering the size and geometric structure of peripheral macrocyclic *** with the occurrence of a single-electron reduction,these macrocycleencircled dicopper complexes show distinct electron transfer pathways as a function of differently sized and substituted macrocyclic *** structural characterization and density functional theory calculations reveal that a coupled metal-ligand and bimetallic cooperativity is involved in the singleelectron reductionof hydroxyl-bridged dicopper species within macrocyclic homologue ligands Py[7]Ph[1]and Py[7]Ph[1]-*** highly flexible configurations of macrocyclic ligands are conducive to stabilizing copper-oxygen intermediates with different valence states and facilitating an intramolecular electron transfer between macrocyclic ligands and the central copper-oxygen *** of biased electron transfer behaviors of copper-oxygen species with their peripheral macrocyclic ligands provides a new means of tuning redox properties of metal cluster species and opens a broader prospect on the mechanistic study of copper-containing enzymes and copper-catalyzed transformations.