Meet our Spring 2022 Student Marshals:
The Department of Biochemistry and Molecular Biology is proud to recognize Bryce Katch as a Student Marshal for the 2022 Spring Commencement! Bryce is a graduate of Manheim Township High School in Lititz, Pennsylvania. He is a Dual major in the Biochemistry Option of Biochemistry and Molecular Biology and Chemical Engineering. He has also earned a spot on the Dean’s List a remarkable eight times throughout his undergraduate career.
After graduation Bryce plans to take a gap year where he will be conducting research at Memorial Sloan Kettering Cancer Center. During his time at the Cancer Center he plans to apply to both MD/PhD programs.
Congratulations Bryce on being named a Spring 2021 Student Marshal, and also for serving as a wonderful of example of why We Are Penn State!
Read more, below, about Bryce’s remarkable undergraduate career.
Commencement Faculty Escort:
- Dr. Amie Boal
What impact has working with Dr. Amie Boal has on your undergraduate career, and your future career specifically?
Dr. Boal has been an amazing mentor throughout my undergraduate experience. I joined her lab in the fall of my sophomore year, and I also had the opportunity to take BMB 401 with her that same fall. Dr. Boal is both a phenomenal researcher and dedicated teacher, so I really feel fortunate to have been in both her lab and her classes. I hope to take the same passion for science that she has with me throughout my career. Working in her lab has also informed my future research goals; I'm hoping to get my PhD in a lab that incorporates biochemistry with medicine.
Several members of the Boal lab (and the larger bioinorganic group) have also had a major impact on my undergraduate career. I have had the privilege of being mentored by several people in lab- Pedro Rivera-Pomales (Boal Lab grad student), Laura Collazo-Perez (Boal Lab grad student), and Jeff Slater (Bollinger-Krebs lab postdoc). My mentors have all been incredibly supportive and helpful throughout my time doing research on the 3rd floor.
What is the most important lesson/memory/observation that you will take with you from your time at Penn State?
I would say that the overall lesson I learned was to have things you love to do outside of school/work, because I feel that it keeps me grounded and is a good way to take my mind off things. I will definitely keep this lesson in mind as I move forward in my career!
Undergraduate Honors and Awards, Extracurricular Activities, and Honorary Society Memberships:
- Barry M. Goldwater Scholarship (2021)
- Evan Pugh Scholar Award (2021, 2022)
- President Sparks Award (2020)
- President’s Freshman Award (2019)
- Penn State Marching Blue Band (4 years)
- Penn State Engineering Ambassadors (2 years)
- Penn State Saxophone Studio (4 years)
In what laboratory did you conduct your research?
- Dr. Amie Boal
What was your research topic, and can you describe for our audience your research activities?
My work is focused on understanding in detail how enzymes perform chemistry. The chemical reaction I have studied throughout undergrad is known as halogenation, and enzymes that perform this reaction are known as halogenases. This reaction involves the direct formation of carbon-halogen bonds. These bonds are critical in synthetic chemistry and also give drugs many desirable properties. The existing ways to perform this reaction without the use of enzymes often require environmentally hazards solvents and produce unwanted byproducts. Therefore, there is significant interest in understanding how enzymes can perform this chemistry so that we can harness it for practical applications. My work has been centered on two questions:
- How can we introduce halogenation activity into enzymes that do not normally perform this reaction?
- What is the underlying mechanism for enzymes that natively perform halogenation?
To answer these questions, I used a variety of techniques that inform us about enzyme function.
Enzymes are proteins that catalyze chemical reactions, and we know that their function is often strongly linked to their three-dimensional structure. Thus, one way to gain insight into enzyme function is with a technique known as X-ray crystallography, which allows us to solve an enzyme's three-dimensional structure. If we can get X-ray data at multiple points throughout an enzyme's reaction, we can "watch" an enzyme as it performs chemistry. I used this technique to understand how the structure of an enzyme could enable it to perform halogenation.
To "put the puzzle pieces together," I also used a variety of other biochemical techniques. Proteins absorb light at distinct wavelengths, and often, different points in an enzymatic reaction can be identified based on the absorption profile across different wavelengths. This approach is generally known as absorption spectroscopy. I used this approach to investigate how different substrates can bind to and react with halogenase enzymes. I also sought to determine the specific products made by the enzymatic reaction, which can be done with liquid chromatography-mass spectrometry (LC-MS). Both of these techniques helped us to construct a more complete picture of how this enzymatic reaction is performed.