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KALAMAZOO, Mich.—A scientific breakthrough a century in the making has landed a ÃÛÌÒÉçÇø Michigan University faculty member a prestigious National Science Foundation (NSF) CAREER Award. Dr. Ricky Stull, assistant professor of chemistry, earned the five-year $757,000 grant for a project that could impact future biotechnology development.

"This award is only given to the top early career faculty in their field, and it is a testament to the great work Dr. Stull is doing as well as the caliber of faculty we have here at ÃÛÌÒÉçÇø Michigan University," says Dr. Remzi Seker, vice president for research and innovation. "It's also so beneficial for our students, the future innovators, to have the opportunity to engage in this type of research, which has the potential to have a tremendous impact on the field."

Stull plans to study a family of enzymes known as flavoprotein amine oxidases (FAO), which generally use molecular oxygen as a catalyst for biochemical reactions, to determine if any of them buck that tradition.

The project builds on a 2021 discovery by his laboratory of a nicotine-degrading enzyme called NicA2 that has the potential to help smokers overcome addiction. In that case, he and researchers in his lab determined NicA2 uses a protein called cytochrome c instead of oxygen.

"It's a pretty cool feeling to think we thought the case was closed on this—everything acts this way, it's done—but it turns out that's not true," says Stull. The breakthrough contradicted nearly 100 years of research on the FAO enzyme family, which hypothesized more than 100,000 similar enzymes behaved the same way. "That's the cool thing about science: We're constantly making new discoveries and revising old hypotheses and assumptions. So, it's really fun to stumble upon a discovery like this."

Turns out the scientific method pairs well with beer, as Stull and colleague Dr. Todd Barkman, professor of biological sciences, began to hypothesize over hops at the local pub.

"He and I talked about our results over beers many times, wondering are there other enzymes that are similar to this nicotine-degrading enzyme that don't fit the mold? And how could we go about finding them?" Stull says. "So we combined his expertise with my knowledge about enzymes in this family that seem highly suspicious, and we found more than 100."

Determining why the enzymes have evolved to reject molecular oxygen could help researchers find new ways to engineer biotechnology to be more effective.

Undergraduate students in Stull's biochemistry laboratory classes will have the opportunity to actively participate in the research alongside the students in his research lab and potentially be included in published papers related to discoveries.

"They'll get the experience of exploring something that is completely unknown, that we have no idea what the answer will be, because no one's ever done it before," he says.

Stull also plans to use his CAREER grant to develop a platform to make it easier for federal work-study recipients to connect with faculty mentors and use their funds to complete undergraduate research.

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