Marquette professors receive $525,000 grant to research a new 'green' catalyst
November 15, 2018
MILWAUKEE — Dr. Richard Holz, Dean of Marquette University's Way Klingler College of Arts and Sciences and professor of chemistry, and Dr. Brian Bennett, professor and chair of physics, have received a $525,000 grant from the National Science Foundation to continue research into enzymes that are a new type of "green" catalyst.
Holz and Bennett will use Marquette's electron paramagnetic resonance spectrometer along with kinetic analyses, biochemical and computational chemistry methods, and X-ray crystallography to learn more about how nitrile hydratases convert nitriles, an organic compound found in plants, to amides.
"The major impediment to understanding the biological roles and possible bioremediation processes for nitriles, is the lack of understanding of the catalytic mechanism of nitrile hydratases," Holz said.
The enzyme that catalyzes this chemical reaction has proven useful in the cleanup of nitrile-based chemicals and pesticides from the environment and is recognized as a new type of "green" catalyst. The researchers hope their work leads to development of new bioremediation catalysts.
In addition, these enzymes are used in organic chemistry labs and in the production of acrylamide (a chemical used in making paper, dyes and plastics, and in treating drinking water and wastewater) and nicotinamide (a form of vitamin B3 found in food and used as a dietary supplement).
Learning more about the catalytic mechanism of nitrile hydratases, which underscore their chemical reactivity, could lead to the development of new biocatalysts, the researchers said.
"These biocatalysts operate in water at ambient temperatures and pressures. They are exquisitely specific and promise environmentally friendly syntheses with 100 % efficiency for chiral pharma compounds in the future," said Bennett.
About the Holz Research Group
The team researches bioinorganic chemistry, mechanistic enzymology and biophysical chemistry. It studies the structure/function of metalloenzymes, some of which are important industrial catalysts or antimicrobial targets.
About the Bennett Lab
The lab uses electron paramagnetic resonance (EPR) of biopsy tissue at liquid helium temperatures to investigate the metabolic effects of cancer, mitochondrial diseases, and therapies; and employs EPR spectrokinetics of metalloproteins such as nitrile hydratase, and computational methods, to characterize reactive transient species.