Active sites of proteins containing metal–oxo and hydroxo units are proposed to have important effects in metallobiochemistry. In many cases, they have been proposed to be key intermediates during catalysis, especially in proteins that utilize dioxygen for oxidative transformations. In addition, it has been proposed that intermediates formed during water oxidation at the oxygen-evolving complex within Photosystem II contain both metal–oxo and metal–hydroxo units. Developing synthetic systems having similar units has been challenging because of difficulties in replicating the structural components associated with active sites in metalloproteins. We develop artificial systems that duplicate some of the structural complexity found in proteins, including hydrogen bonding networks that control the local environment around metal ions. This talk will describe our latest efforts in preparing and characterizing new metal-oxido and hydroxido complexes with a variety of biologically relevant metal ions. Included in the discussion will be methods to prepare both low- and high-valent Mn and Fe complexes containing terminal hydroxido and oxido ligands. Our work suggests that high spin metal-oxo species can have a role in a variety of biochemical processes, including C–H bond activation.

Metal-oxido and metal-hydroxido complexes in biology

255th National Meeting (2018)

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