Brent A. Fallin
Honors in Physics: Analysis of the Reaction Between Nitric Oxide and Sickle Cell Hemoglobin Using Mössbauer Spectroscopy
The goal of my research this past year has been to use Mössbauer Spectroscopy to analyze the reaction between nitric oxide (NO) and deoxygenated sickle cell hemoglobin (deoxy-Hb-S). Preliminary research on this topic was first undertaken by Christopher McCracken last year in partial fulfillment of the requirements for Honors in Physics at Hampden-Sydney College. McCracken sought to determine the binding site for NO in the complex hemoglobin molecule. One potential site was one of the four iron atoms contained in hemoglobin. An analysis of the reaction between NO and deoxy-Hb-S using Mössbauer Spectroscopy provides an easy way to either verify of disprove the iron in hemoglobin as the NO binding site. McCracken’s final data provided encouraging evidence that the NO does indeed interact with the iron. However, because of low detector count rates and a small number of available spectra, his research results did not imply a definitive answer to the binding site question. The current research has focused on further analysis of McCracken’s sample of Hb-S in NO. A statistically meaningful (>1*106 counts) Mössbauer spectrum of the sample was taken and an complete analysis was then performed. The final results from the spectrum were then compared with existing Mössbauer data of normal hemoglobin and with McCracken’s prior data in order to examine changes in the Hb-S over time and to look for potential NO binding. It is greater goal of this continuing project that the current as well as future results may ultimately prove useful to the scientific and medical community at large.