RESEARCH IN BRIEF
INSTRUMENTAL ARRIVAL When a newly arrived professor helped upgrade a key device, his wasn’t the only research that benefited. When biophysicist Dr. Brian Bennett arrived to chair the Physics Department in 2014, he was pleased to find a researchgrade electron paramagnetic resonance spectrometer, donated just six months prior. Valued for providing detailed information on the geometric and electronic structure of molecular and solid-state materials, the spectrometer nevertheless came equipped with difficult-torepair analog technology that offered somewhat limited applications.
Professor and Chair, Physics
Assisted by Klingler College of Arts and Sciences Dean Richard Holz, Bennett — a 25year veteran of EPR research — secured funding from the National Science Foundation to rebuild the instrument with new digital components. The upgrade extended the device’s life expectancy by 20 to 25 years, Bennett says, and added a modern low-temperature cooling system that doesn’t require liquid helium.
Dr. Brian Bennett
“We are the only research university in the Midwest with this capability,” says Bennett, who got the project over the goal line by covering additional costs with
With four partnering institutions — including the Medical College of Wisconsin, where he spent 13 years on the faculty — Bennett is now using the spectrometer to develop an accurate diagnostic method for mitochondrial disease, a severe and often fatal condition in children that has no cure, but responds to some treatments. Their first research paper was published last year. Although there is no established way to distinguish between two manifestations of the disease, which vary widely in risks posed to patients, Bennett says, “Our technique tells you very straightforwardly whether you’re getting a free radical buildup, which is very toxic, or whether it’s simply that the mitochondrial chain is not working to produce enough energy (as ATP) to fuel the body’s requirements.” Bennett’s other focus is a longtime NSF-funded collaboration to study the chemical mechanism of nitrile hydratase, an enzyme with high potential for making novel pharmaceutical components in an environmentally friendly way. Using a technique called rapid-freeze quench, researchers mix the enzyme with various chemicals for milliseconds and then use the spectrometer to provide “snapshots during the course of the reaction and conceptually build a movie of how it does the chemistry that it does.” PAULA WHEELER
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his own research dollars and Marquette matching funds. Now, fellow pure- and applied-science researchers can conduct very low-temperature experiments on campus at “absolutely enormous” cost savings, he says, while regional research powerhouses may be paying up to $2,000 a week for liquid helium.
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