Research

Research involved investigations into the structure and mechanism of oxalate oxidase. Oxalate oxidase catalyzes the oxygen-dependent oxidation of oxalate to carbon dioxide in a reaction that is coupled with the formation of hydrogen peroxide. Although there is currently no structural information available for oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx), sequence data and homology modeling indicate that it is the first manganese-containing bicupin enzyme identified that catalyzes this reaction. Interestingly, CsOxOx shares greatest sequence homology with bicupin microbial oxalate decarboxylases (OxDC).

The tools of bioinformatics and computational biology broadened our understanding of the complex relationship between sequence, structure, and function in the mechanistically diverse cupin superfamily.

Membrane inlet mass spectrometry, isothermal titration calorimetry, circular dichroism, electron paramagnetic resonance spectroscopy, site-directed mutagenesis studies, enzymatic assays, column chromatography, and protein purification and characterization informed our studies.