William (Will) Parsons

(he/him/his)

  • Associate Professor of Chemistry and Biochemistry

Areas of Study

Education

  • PhD, Stanford University, 2013
  • BA, Williams College, 2007

Chemical biology, small-molecule synthesis, intramembrane hydrolases

Enzyme-mediated hydrolysis is a ubiquitous component of numerous metabolic pathways in the body. Nature has developed a number of chemistries within hydrolase active sites to cleave a diverse array of biological substrates. The Parsons lab studies enzymes that use serine and threonine residues to catalyze turnover of their substrates. A subset of these enzymes with intramembrane active sites are of particular interest due to their unique biochemistry as well as their involvement in pathways underlying metabolic and neurological diseases, including Parkinson’s disease and type 2 diabetes. 

The Parsons lab exploits the active site chemistry of these hydrolases to create new chemical probes for this enzyme class. Drawing upon methodology from synthetic chemistry, biochemistry, molecular biology, and medicinal chemistry, research in the Parsons lab focuses on the development of small molecule tools to study the physiological roles of intramembrane hydrolases.

Prof. Parsons teaches general and organic chemistry courses in the department. He is on leave during the fall semester of 2024. During the spring semester of 2025, he will be teaching lecture and lab sections of CHEM 205: Principles of Organic Chemistry and a lab section of CHEM 254: Bioorganic Chemistry.

(Note: An asterisk indicates an Oberlin student/graduate co-author)

  • Davies CC*, Hu R-M, Kamitsuka PJ*, Morais GN*, Gonzalez RS*, Bustin KA, Matthews ML, Parsons WH. "Activity-based protein profiling of RHBDL4 reveals proteolysis of the enzyme and a distinct inhibitor profile." ACS Chem Biol 202419, 1674–1682. doi: 10.1021/acschembio.4c00273.
  • Parsons WH, Cravatt BF. "Activity-based protein profiling." In Advanced Chemical Biology: Chemical Dissection and Reprogramming of Biological Systems; Hang HC, Pratt MR, Prescher JA, Eds; Wiley-VCH, 2023; pp 503–526.
  • Wang X, Lin Z, Bustin KA, McKnight NR, Parsons WH, Matthews ML. “Discovery of potent and selective inhibitors against protein-derived electrophilic cofactors.” J Am Chem Soc2022144, 5377–5388. doi: 10.1021/jacs.1c12748.
  • Parsons WH, Rutland NT*, Crainic JA*, Cardozo JM*, Chow AS*, Andrews CL*, Sheehan BK*. Development of succinimide-based inhibitors for the mitochondrial rhomboid protease PARL. Bioorg Med Chem Lett. 202149, 128290. doi: 10.1016/j.bmcl.2021.128290.
  • Lin Z, Wang X, Bustin KA, Shishikura K, McKnight NR, He L, Suciu RM, Hu K, Han X, Ahmadi M, Olson EJ, Parsons WH, Matthews ML. Activity-based hydrazine probes for protein profiling of electrophilic functionality in therapeutic targets. ACS Cent Sci. 20217, 1524–1534. doi: 10.1021/acscentsci.1c00616.

Complete List of Publications

Spring 2025

Principles of Organic Chemistry — CHEM 205
Bioorganic Chemistry — CHEM 254

Notes

William Parsons publishes with six recent graduates

August 4, 2021

William Parsons, assistant professor of chemistry and biochemistry, and six recent Oberlin graduates (Charlotte Andrews '19, Joaquin Cardozo '20, Alyssa Chow '20, Jennifer Crainic '20, Nicholas Rutland '20, and Brendan Sheehan '19) published an article title "Development of succinimide-based inhibitors for the mitochondrial rhomboid protease PARL" in Bioorganic & Medicinal Chemistry Letters.

News

The Forever Impact of Zach Smith ’26

October 4, 2024

Zach Smith ’26 is a chemistry major with a business concentration. This summer, he interned at CoreWater Technologies, an Oberlin-based company whose mission is to eliminate chemicals forever from our drinking water. Here, he discusses what he did, how he got there, and his hopes for the future.

Winter Term in Oberlin: 2020

February 24, 2020

Winter Term is a time of year when Oberlin students are encouraged to conduct independent or group projects outside of courses related to their majors. Pursuits can be done on or off campus with students choosing to work almost anywhere on the map. This year we highlight some of the work by the more than 900 students who completed projects in Oberlin.