Arden Clauss

Around fifty percent of known proteins associate with metal ions, and organic cofactors are pervasive among oxidoreductases. In natural systems these two aspects come together rarely and are often hard to work with, so controllable modelling using artificial metalloenzymes (ArMs) is quite powerful. Pyrroloquinoline quinone (PQQ) is a redox cofactor found in dehydrogenase enzymes, and recently we modified the periplasmic binding protein PqqT to create a PQQ-lanthanum active site with oxidoreductase activity. This system is tractable and presents two interesting avenues of investigation: modelling of natural quinoprotein dehydrogenases and engineering new ArM biocatalysts. We are currently building a comprehensive description of the PqqT ArMs behavior with the goal of using metal-dependent enzymatic redox cofactors to conduct otherwise challenging multi-electron reactions.