Accessing a synthetic Fe^IIIMn^IV core to model biological heterobimetallic active sites.

ABSTRACT: Metalloproteins with dinuclear cores are known to bind and activate dioxygen, with a subclass of these proteins having active sites containing FeMn cofactors and activities ranging from long-range proton-coupled electron transfer (PCET) to post-translational peptide modification. While mechanistic studies propose that these metallocofactors access Fe^IIIMn^IV intermediates, there is a dearth of related synthetic analogs. Herein, the first well-characterized synthetic Fe^III-(μ-O)-Mn^IV complex is reported; this complex shows similar spectroscopic features as the catalytically competent Fe^IIIMn^IV intermediate X found in Class Ic ribonucleotide reductase and demonstrates PCET function towards phenolic substrates. This complex is p

SUBMITTER: Lee JL 

PROVIDER: S-EPMC10882444 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature