Associate Professor of Chemistry
Penn State Behrend
Mary Grace I. GalinatoDr. Galinato teaches general and physical chemistry, and is a bioinorganic/biophysical chemist by training. Broadly speaking, her lab focuses on two systems: naturally- and artificially-occurring heme enzymes; and synthetic oligourea foldamers, a group of polymers which model the secondary structures of enzymes.

A) Nitrite reductase activities of globin and related enzymes

Nitric oxide (NO), a signaling molecule, plays critical roles for proper body functions at the right amounts but is implicated in various health problems when present in excess. The delicate balance of NO concentrations in the body is controlled by enzymes that eliminate this molecule when in excess, and generate it when required. One group of enzymes that has gained recent attention for its unique role in producing NO through NO2- reduction is the globin family, in particular myoglobin (Mb) and hemoglobin (Hb). Although the mechanism of the reaction between deoxyMb (deoxyHb) and nitrite is unclear, it is postulated to follow that of cd1 nitrite reductases. Her group aims to investigate the fundamental chemistry between globins and nitrite. Results generated from her lab ultimately allows for the design enhanced catalysts based on the nitrite reductase activity of Mb in particular, providing a novel means for controlled generation of nitric oxide.

B) Conformational preferences of oligourea foldamers

Another thrust in her research lab involves the investigation of foldamers, a synthetic group of polymers that folds into well-defined secondary structures in solution, and have biomedical, material science, and catalytic applications. Her group aims to elucidate the conformational properties and dynamic behavior of foldamers, both of which influence their structural organization. In particular, they focus on oligourea foldamers whose basic motif consists of repeating units of substituted N,N’-diphenylurea. A systematic study of the monomeric units with varying structural features will allow them to determine the driving forces that induce a particular conformation within a specific solvent environment. They approach this study by using combined experimental and computational studies, providing quantitative structural information, energetics, and conformational preferences in solvents with varying polarity.

Department of Chemistry
School of Science
Penn State Behrend
4205 College Drive
Erie, PA 16563-0203
Created by: C.V.L.
Maintained by: M.G.I.G.
Hammermill 32
Office: 814.898.6004
Fax: 814.898.6213
Penn State Erie, The Behrend College