Our lab will focus on designing metal-dioxygen and metal-oxyl cores (M = Cu, Ni, Co, Ru, W) to mimic the reactivity and fundamental aspects of non-heme metalloenzyme active sites, particularly those with unclear or unknown mechanisms. To address this, we will generate synthetic model systems and investigate their spectroscopic, structural, kinetic and electrochemical properties at low-temperature (<-80 °C) to elucidate reaction pathways and provide crucial insights into bio-inspired catalyst design. In addition, DFT calculations will be carried out within our group to gain a deeper understanding of the electronic structures of short-lived intermediates, as well as their associated thermodynamic and kinetic parameters. Special emphasis will be placed on redox-active ligand architectures that offer both steric and electronic control at the metal center, enabling selective O2 coordination and incorporating subtle 2nd-sphere interactions commonly found in enzymatic systems. Looking ahead, we also aim to explore heterobinuclear iron-peroxo-copper complexes, which are relevant to the active site chemistry of cytochrome c oxidase.