The power of using continuous-wave and pulsed electron paramagnetic resonance methods for the structure analysis of ferric forms and nitric oxide-ligated ferrous forms of globins.
For several decades now, electron paramagnetic resonance (EPR) has been a valuable spectroscopic tool for the characterization of globin proteins. In the early years, the majority of EPR studies were performed using standard continuous-wave EPR techniques at conventional microwave frequencies. In the last years, the field of EPR has known tremendous technological developments, including the introduction of advanced pulsed EPR and high-frequency EPR techniques. After a short overview of the basics of EPR and recent advances in the field, we will illustrate how these different EPR methods can provide information about the dynamics and geometric and electronic structures of heme proteins. Although the main focus of this chapter lies on the EPR analysis of nitric oxide-ligated ferrous heme proteins and ferric heme systems, we also briefly outline the possibility of site-directed spin labeling of heme proteins. The last section highlights the future potential and challenges in using this magnetic resonance technique in globin research.
Van Doorslaer
Sabine
S
University of Antwerp, Department of Physics, SIBAC Laboratory, Antwerp, Belgium.
Desmet
Filip
F
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D005914:Globins / Q000737:chemistry* / Q000378:metabolism; D006420:Hemeproteins / Q000737:chemistry; D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D013194:Staining and Labeling / Q000379:methods
D006420:Hemeproteins; D009569:Nitric Oxide; D005914:Globins; D007501:Iron