Since my Post-Doctoral UMDF accelerator runner-up award, I have transitioned to the position of Staff Scientist in the Pagliarini Laboratory at Washington University in St. Louis. In this role, I am excited to continue to study open questions in coenzyme (CoQ) biosynthesis, while using my expertise in biochemistry and mass spectrometry to support existing, impactful projects in the lab while also mentoring the next generation of scientists.

During my UMDF fellowship, I worked on a collaborative project to understand how the uncharacterized protein COQ9 contributes to CoQ biosynthesis and supports the formation of complex Q. Using cryogenic electron microscopy, we have provided the first structural characterization of a subcomplex of CoQ proteins: COQ9 and COQ7. This structure, along with molecular dynamics simulations, supports a model in which COQ9 cooperates with COQ7 to access CoQ precursors within the mitochondrial membrane to coordinate synthesis steps to produced mature CoQ. We have communicated these findings in a manuscript that has been recently accepted at Molecular Cell [a peer-review research journal] and will be published soon.

We have been interested in studying CoQ as its deficiency is a hallmark of mitochondrial disorders, yet many details of its transport remain unclear, thus thwarting the development of new, more effective CoQ-based therapeutics that don’t suffer from the same poor bioavailability of CoQ itself. By understanding how proteins come together at a structural level to make CoQ, we hope to gain insight to ways in which we could re-stabilize an unstable complex Q or bypass broken biosynthetic pathways in order to therapeutically address CoQ deficiencies for patients with mitochondrial disorders.