Heterobimetallic complexes bridged by oxygen-derived ligands have been of interest to synthetic inorganic chemists for some time due to their rich spectroscopy and unique structural features. Recently, hetero-bimetallic cofactors comprised of Fe and Mn have been shown to activate O2 in enzymes such as RNR 1c and R2lox. The Fe/Mn cofactor in RNR 1c forms a stable oxidant that is responsible for initiating the free radical mechanism by which ribonucleotides are reduced to deoxyribonucleotides in Chlamydia trachomatis. The function of R2lox is currently not well understood, but it has been proposed that the Fe/Mn cofactor is responsible for forming a unique crosslinked Val-Tyr residue in the protein scaffold. This has led to an effort to synthesize heterobimetallic compounds that contain Fe and Mn that can mimic proposed intermediates in the oxygen activation process. Our group’s recent work has shown that FeIV(O) compounds react with di-valent metal salts and complexes to form FeIII–O–MIII compounds. To mimic the Fe/Mn active sites, FeIII–O–MnIII complexes have been synthesized using the reported method. These new compounds have labile sites that allow them to react with H2O2 and generate peroxo adducts. These adducts have been studied by a variety of spectroscopies (resonance Raman, XAS, UV-Vis and EPR) in order to give insight to the structures of compounds related to intermediates involved in enzymatic oxygen activation.

Synthesis and characterization of heterobimetallic Fe–O–Mn complexes: Modeling RNR 1c and R2lox

2019 Fall National Meeting

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