Metal ions are ubiquitous in biology and aid in many enzymatic transformations. For instance, high valent iron–oxido and –hydroxido species are proposed to be key intermediates in oxidative processes catalyzed by non–heme iron proteins. A subclass of these proteins contains diiron cores that includes ribonucleotide reductase and the hydroxylase component of methane monooxygenases. To investigate the properties of bimetallic cores, we have developed a symmetric tripodal ligand framework containing phosphinic amido groups, which can stabilize high–valent metal centers, provide an auxiliary site for the coordination of the second metal ion, and facilitate intramolecular hydrogen-bonding/proton-shuttling. This presentation will describe the preparation, molecular structures, and physical properties for new bimetallic iron species. These di-Fe complexes have different primary coordination spheres that allowed formation of a series of complexes with distinct [FeII–(μ–OH)–FeIII], [FeIII–(μ–O)–FeIII], and [FeIII–(μ–O)–FeIV] cores.

Synthetic models for metalloenzyme active sites: Accessing high valent non–heme diiron complexes

ACS Spring Meeting 2021

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