In this project supported by the Experimental Physical Chemistry Program of the Chemistry Division and the Molecular Biophysics Program of the Division of Molecular and Cellular Biosciences, Gilbert Walker of the University of Pittsburgh will study the structure and dynamics involved in the binding of nitric oxide with cysteinyl binding sites in serum albumin (SA) and glutathione. The proposed work will employ state-of-the-art transient and static, infrared and visible, and linear and circular dichroism spectroscopies. The conformational information resulting from these studies will aid in understanding the mechanisms of thermolytic nitric oxide release processes at cysteines. These experiments will be compared to ab initio theoretical predictions of the optimized cysteine-NO geometry and potential energy surface.
The proposed project will help understand how the molecular structure of proteins affects their ability to bind with substances, called ligands, and how these ligands affect long-range signaling in the proteins. Proteins such as those studied here, which contain the cysteine residue, are principal scavengers of nitric oxides in living systems. Nitric oxides are among the gases that are important in atmospheric ozone destruction and global warming. Escape of these gases from microbes during waste water treatment, for example, is also a concern in industrial processing.
