Metalloproteins catalyze nitric oxide (NO) chemistries in bioenergetics pathways, natural product biosynthesis pathways, and to protect against cell damage caused by nitrosative stress. Our lab is interested in the mechanisms of oxidative NO-dependent metalloenzymes involved in natural product biosynthesis and nitrosative stress protection. Understanding the mechanisms of these enzymes will enable the engineering of nitration biocatalysts and provide insight into how human pathogens evade the human immune response.

Essential across all domains of life, enzymes often expedite challenging biological reactions by incorporating transition metal ions whose oxidation and spin states are coordinated with changes in atomic structure. While great strides have been made in the field of metalloenzymology, our understanding of these dynamic processes remains limited as the timescales on which they occur render visualization technically challenging.

The diverse post translational modifications (PTMs) add up the already enormous in number, meanwhile low abundance for certain species of proteomes with even more complexity. As efforts to enrich peptides and proteins of interest out of complex mass spectral background, various fractionation, separation, enrichment, and feature detection strategies are extensively implemented.

As the population and its demand for electricity increases, the call for renewable energy has been growing ever louder. Unfortunately, these energy sources (namely wind and solar power) can not always meet real-time needs. In order to gain the most from these energy sources while being able to cover their gaps in production, the need for storage of excess energy at the grid-level has become apparent.

Dendritic cells (DCs) are the most effective type of antigen-representing cells (APCs).^[1] DCs capture tumor antigens, process them, and migrate to the T cell zone in tumor-draining lymph nodes (TDLNs) where they prime T cells through cross-presentation.

Carotenoid cleavage dioxygenases (CCDs) are mononuclear non-heme iron enzymes that classically split carotenoids at specific alkene bonds producing apocarotenoid products. Certain members of this enzyme superfamily have evolved to process alternative substrates with varying regio- and stereo-selectivity, and some catalyze alternative reactions including alkene geometric isomerization and ester hydrolysis.

IMPORTANT: Instructor assignments for sections of General and Organic Chemistry are subject to change at any time.  This course schedule is for planning purposes only; Athena is the official source of record for available course offerings.

Please note that a single course may have multiple meeting times and locations, and be sure to factor that into your schedule planning.