Tuning the Diiron Core Geometry in Carboxylate-Bridged Macrocyclic Model Complexes Affects Their Redox Properties and Supports Oxidation Chemistry
| Autor: | Stephen J. Lippard, Mikael A. Minier, Fang Wang, Megan N. Jackson, Andrei Loas, Sabine Becker |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
chemistry.chemical_classification
010405 organic chemistry Stereochemistry Carboxylic acid Geometry Methane monooxygenase hydroxylase 010402 general chemistry 01 natural sciences Redox 0104 chemical sciences Inorganic Chemistry Turn (biochemistry) chemistry.chemical_compound Ribonucleotide reductase chemistry Moiety Carboxylate Physical and Theoretical Chemistry Phosphine |
| Zdroj: | Inorganic Chemistry. 56:11050-11058 |
| ISSN: | 1520-510X 0020-1669 |
| DOI: | 10.1021/acs.inorgchem.7b01418 |
| Popis: | We introduce a novel platform to mimic the coordination environment of carboxylate-bridged diiron proteins by tethering a small, dangling internal carboxylate, (CH2)nCOOH, to phenol-imine macrocyclic ligands (H3PIMICn). In the presence of an external bulky carboxylic acid (RCO2H), the ligands react with [Fe2(Mes)4] (Mes = 2,4,6-trimethylphenyl) to afford dinuclear [Fe2(PIMICn)(RCO2)(MeCN)] (n = 4–6) complexes. X-ray diffraction studies revealed structural similarities between these complexes and the reduced diiron active sites of proteins such as Class I ribonucleotide reductase (RNR) R2 and soluble methane monooxygenase hydroxylase. The number of CH2 units of the internal carboxylate arm controls the diiron core geometry, affecting in turn the anodic peak potential of the complexes. As functional synthetic models, these complexes facilitate the oxidation of C–H bonds in the presence of peroxides and oxo transfer from O2 to an internal phosphine moiety. |
| Databáze: | OpenAIRE |
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