Vanadium haloperoxidases (VHPOs) are a class of redox enzymes characterized by their vanadate-dependent active site and are named for their ability to catalyze the aqueous two-electron oxidation of halide ions.  Various research groups have designed different metal-organic compounds with the intention of mimicking the structure and function of the active peroxidated form of VHPOs.  The most studied mimic compound is K[VO(O2)(heida)], a vanadium peroxo-oxo compound chelated with N-(2-hydroxyethyl) iminodiacetic acid (heida).In this study, we have demonstrated that there are significant structural and reactivity differences between the active site of supported vanadium oxide catalysts and the K[VO(O2)(heida)] complex.  We have used in-situ Raman, UV-Vis, and ATR-IR spectroscopy during aqueous methanol oxidation to examine K[VO(O2)(heida)]. This study elucidates the K[VO(O2)(heida)] catalytic active site, reaction intermediates, and the important role of the vanadium peroxo structure.  These studies will be used as a benchmark for future studies of vanadium haloperoxidase (VHPO) enzymes.

Bridging the gap between heterogeneous and enzyme catalysis:   In situ spectroscopic study of vanadium haloperoxidase enzyme functional mimics

243rd National Meeting (2012)

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