Broadly speaking, we are interested in the investigation of metalloprotein structure, function and dynamics. One focus in the lab is on proteins that participate in iron homeostasis in pathogenic bacteria. A key factor in the successful colonization by pathogenic microbes is their ability to acquire iron, an essential nutrient that plays critical roles in biological systems. Iron is tightly regulated, and bacteria have evolved a variety of mechanisms to scavenge iron from their host organisms. We use spectroscopic, computational and structural and molecular biology techniques to investigate heme degradation proteins and transcriptional regulatory proteins that function in the bacterial acquisition of iron.
Another focus of the work in the Bowman lab is using NMR spectroscopy to study biomolecular structure and dynamics. A current project is determination of the structure of YfiD, a protein that is homologous to the glycyl radical-containing C-terminal region of pyruvate formate lyase (PFL), which functions to convert pyruvate into acetyl-CoA. We hypothesize that YfiD functions to restore activity to PFL after cleavage of part of the PFL enzyme. Our goal is to elucidate a structural model of YfiD in solution.
Member of Integrated Biosciences Graduate Program (Chemical Biology)