This U.S.-Hungarian research project between Jane Vanderkooi of the University of Pennsylvania, Philadelphia, and Judit Fidy of Semmelweis University, Budapest, will examine chromophore/protein matrix interactions of functional significance in plant peroxidase systems. Their approach involves a combination of computational and high-resolution vibrational and electronic spectroscopic methods and features two peroxidases whose structures are known: horseradish peroxidase and yeast cytochrome c peroxidase. If successful, results should contribute to our basic understanding of biophysics and the biochemistry of heme proteins, a family of enzymes that catalyze the oxidation of aromatic compounds by hydrogen peroxide.
Planned experiments include: 1) binding studies using low temperature adsorption and laser fluorescence line narrowing to probe coupling between chromophore and protein matrix; 2) Fourier transform infrared spectroscopy to probe matrix conformational heterogeneity and the heme geometry, and 3) molecular dynamics to model substrate binding and docking in conjunction with electrostatic calculations. These are expected to show the interaction between prosthetic group and apoprotein as well as the functional significance of structural and conformational heterogeneity.
This project in molecular biophysics fulfills the program objective of advancing scientific knowledge by enabling experts in the United States and Central Europe to combine complementary talents and share research resources in areas of strong mutual interest and competence.
