Participating Faculty Members
Updated for 2014
Dr. John Berberian
My research examines the structure in liquids by probing the electrical and mechanical environment in which the molecules of the liquid move. The motions of these molecules, translational and rotational, are determined by viscosity and dielectric (polarization) measurements as a function of time. Simple molecular systems are used for these studies over a wide range of temperatures, from room temperature down to liquid nitrogen temperatures.
Dr. Jose Cerda
A study of the behavior of heme cofactors in benzene by using cyclic voltammetry
In many heme proteins it has been proposed that the peripheral groups on the heme cofactor have significant interactions with the surrounding protein medium. These heme-protein interactions sometimes define the role of heme cofactor. We plan to thermodynamically characterize the effects of hydrogen bonding to the peripheral substituent groups on heme a and heme b. These effects will be evaluated by measuring the reduction potentials of the hemes in benzene, an aprotic solvent. When compared to other media, the effects of heme-ligand interactions are magnified in benzene. Electrochemical studies will be performed on the “free” heme cofactors, and in the presence of an interacting ligand (bound heme), by using cyclic voltammetry.
The pH Dependence of the UV/Vis-Spectroscopic and Electrochemical Properties of Hemeproteins and their Fluoride-Bound Adducts
The oxidized state of many heme proteins have a water molecule coordinated to the heme iron. However, what is the effect on the midpoint potential of these heme proteins if the water-bound molecule is displaced? In this study, we will measure the UV/Vis-spectroelectrochemical properties of the fluoride-bound heme protein and compared it to those without fluoride.
In our previous studies with myoglobin, we found that there is a difference between myoglobin and its fluoride-bound adduct. From pH 4.7 to 9.0, the midpoint potential of myoglobin shows a decrease of about 20 mV. The decrease in the midpoint potential can be attributed to the binding of the hydroxide ion (OH-). However, the midpoint potential of the fluoride-bound myoglobin is maintained at about 0 mV (vs SHE) from pH 6.4 to 9.0. But, at lower pH, the midpoint potential decreases down to -45 mV (vs SHE) at pH 4.7. We theorized that a conformational change caused by the displaced water is responsible for the drop in the midpoint potential at pH lower than 6.0.
Dr. Mark Forman
The Forman Research Group is interested in the synthesis and study of novel, non-natural products of theoretical interest. During the summer of 2011, a primary goal will be the continued investigation of pentacyclo[4.3.0.02,4.03,8.05,7]non-4-ene, a highly pyramidalized alkene. Specifically, we will investigate alternative synthetic routes to this alkene and study its reaction chemistry. Students in the Forman group will be exposed to a variety of modern synthetic organic techniques including microwave assisted organic synthesis; a broad range of spectroscopic methods, including NMR, FTIR, and MS. Some students may also be exposed computational methods including molecular mechanics.
Dr. Peter Graham
In my laboratory we are investigating transition metal complexes which might catalyze the reaction of carbon dioxide with other simple molecules such as ethylene, hydrogen, or methanol. To this end, my students and I are synthesizing a variety of compounds containing the transition metals tungsten and molybdenum that can coordinate carbon dioxide and activate it towards such reactions. Gaining a better understanding of how such metal complexes interact with carbon dioxide is paramount to developing new catalysts for carbon dioxide utilization.