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Gavin Palowitch

BMMB Graduate Student-Boal Lab
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The Boal Lab

About Me

I attended Ursinus College and received my B.S. in Biochemistry and Molecular Biology in May 2015. I then entered the Penn State BMMB PhD program in the Fall of 2015 and joined Amie Boal’s research group. I have spent the past four years conducting research on essential metal-dependent enzymatic processes in bacteria. Outside of research, I enjoy watching sports, playing drums, and eating delicious food.


Research Interest

My research focuses on metalloenzymes and specifically the enzyme ribonucleotide reductase (RNR). This enzyme is essential for all forms of life because it catalyzes the formation of deoxyribonucleotides, the building blocks of DNA. We are focused primarily on systems found in pathogenic and commensal bacteria in humans and figuring out how they function differently from the human form of the enzyme. We hope that this research will allow for the development of therapeutics that can target these bacteria and avoid side effects.


Research Summary

Our group and collaborators determined crystal structures of bacterial class Ie ribonucleotide reductase (RNR), an enzyme essential for DNA biosynthesis and found exclusively within human pathogens and commensals. Every organism uses an RNR to convert ribonucleotides to the deoxyribonucleotide counterparts needed for DNA replication and repair. The essential nature of these enzymes makes them important drug targets. All known class I RNRs require a binuclear metal cofactor in the β subunit of the enzyme, activated in an oxygen-dependent reaction to form a potent oxidant that drives reaction with substrate in the α subunit of the enzyme. The structure of class Ie RNR shows that some bacteria can use a post-translationally-modified tyrosine amino acid instead of a metal cofactor for aerobic DNA synthesis. The resulting active cofactor for the class Ie RNR is a neutral 3,4-dihydroxyphenylalanine radical (DOPA•). The exact mechanism of installation of this modification remains unknown but requires another protein, NrdI, also characterized by x-ray crystallography in this study. NrdI is a flavin-dependent activase that is proposed to reduce molecular oxygen and shuttle superoxide to the β subunit for cofactor assembly (Palowitch_1). The work reveals a new way that bacteria have adapted to successfully replicate and repair their DNA in the absence of transition metals, one that likely evolved to overcome trace element sequestration imposed by the human immune system. 


Programs and Training Centers


University Committees


Honors and Awards

  • Travel Award #2 – Metals in Biology Gordon Research Seminar - 2019
  • Travel Award #1 – Cell Biology of Metals Gordon Research Conference - 2017
  • Pela Fay Braucher Scholarship - 2016
  • Golden Key International Honour Society - 2016
  • Homer F. Braddock and Nellie H. and Oscar L. Roberts Fellowship - 2015