MroUPO: Small bio-machine, great chemical power, Wenxuan Li G2 and Dali Davis G3 (3937821)
Enzymes have been studied for centuries; however, our knowledge of them is constantly evolving. New enzymes are still being discovered, which opens the door for further studies of enzymatic reactivities and structures. One recently discovered enzyme, an unspecific peroxygenase from the fungus Marasmius rotula (MroUPO), has been of particular interest in the Groves lab. This enzyme, MroUPO, is secreted from the apical part of fungal hyphae and can survive in these extracellular conditions to transform and degrade available organic matters. The fungi can then absorb these degraded matters and use them as an energy source. This fact inspires us to explore how this robust enzyme benefits humans in synthetic and environmental chemistry. Through our experimentation, we were delighted to find that MroUPO can facilitate access to novel oxidized and halogenated building block molecules, reacting with six-, eight- and nine-membered cyclic hydrocarbons to form the remote-site functionalized products. These newly discovered synthetic routes are very important to complement the lack in the current pharmaceutical market and provide inspiration for pollutant disposal. In addition, we saw some dehalogenation occurring on nonactivated aliphatic compounds, which was especially interesting since this type of reactivity is rare in enzymes. Ultimately, we have found novel reactivity patterns from this enzyme, and we hope to continue this work to expand the substrate scope and understand the mechanistic underpinnings that make this enzyme produce such an array of fascinating products.