EPR Characterization of Nitric Oxide Binding to Hemoglobin

  • Yann A. Henry


Since the early work of Hermann (1865) followed by that of Haurowitz (1924), Keilin and Hartree (1937) and Gibson and Roughton (1957)— to point out only a few landmarks—nitric oxide is like O2 and CO, a well-known ligand of deoxygenated reduced hemoglobin.1,2 The complex was first characterized by its red color with large absorbances of the a and b bands of the heme at 574.5 and 536 nm and secondly by a magnetic susceptibility of 3.07 Bohr magnetons,3–5 and by an electron paramagnetic resonance with a g-value close to 2.0.6 The first property was used to reveal the cooperative binding of NO to ferrous iron in an analogous manner to that of O2 and CO;2 the second property, paramagnetism, made NO a choice probe of the physiological O2 binding site. This paramagnetic probe was of great importance at a period (late 60s-early 70s) when X-ray crystallographic data were still at limited resolutions (2.8–3.5 Å) and referred only to the quaternary structure of methemo-globin—instead of oxyhemoglobin due to autoxidation under X-ray beams, as compared to that of deoxyhemoglobin. Other spectroscopic methods such as far-infrared or resonance Raman were then pioneer instruments in the hands of very few scientists, while EPR was more readily accessible.


Nitric Oxide Electron Paramagnetic Resonance Human Hemoglobin Electron Paramagnetic Reso Inositol Hexaphosphate 
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© R.G. Landes Company 1997

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  • Yann A. Henry

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