A Pulsed EPR Investigation of the Hydroxyl 1H Nucleus of Myoglobin Hydroxide

Open Access
Author:
Livada, Jovan
Graduate Program:
Chemistry
Degree:
Master of Science
Document Type:
Master Thesis
Date of Defense:
July 26, 2012
Committee Members:
  • Michael Thomas Green, Thesis Advisor
Keywords:
  • EPR
  • Myoglobin
  • Heme
  • Hyperfine
Abstract:
Pulsed EPR methods have been widely used to characterize the spin environments of bioinorganic cofactors. One of those cofactors is the heme prosthetic group that is found in many biologically important systems such as globins, cytochrome P450s, peroxidases etc. Due to its availability and stability myoglobin is an excellent model heme system. In the effort to characterize a heme spin system and compare the different magnetic resonance techniques, we have undertaken an investigation of myoglobin hydroxide to determine the hyperfine tensor of the hydroxyl proton and in turn estimate the Fe-O distance of the cofactor. In this study, the two- and three-pulse ESEEM, HYSCORE, Davies ENDOR and DFT calculations will be used to elucidate the 1H hyperfine tensor of interest and give insight in to the application of the point-dipole approximation used in magnetic resonance.