EPR Characterization of Nitric Oxide Binding to Hemoglobin

  • Yann A. Henry

Abstract

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.

Keywords

Radar Catalase Hydroperoxide Pyrrole Inositol 

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© R.G. Landes Company 1997

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  • Yann A. Henry

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