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Utilization of Nitric Oxide as a Paramagnetic Probe of the Molecular Oxygen Binding Site of Metalloenzymes

  • Chapter
Nitric Oxide Research from Chemistry to Biology

Abstract

The paramagnetism of many nitrosylated complexes of metalloproteins has led to numerous but limited studies by EPR spectroscopy since the early seventies. Spectral analysis can, in the best of cases, bring evidence of specific structural changes within the metal ligation sphere. However interpretations are somewhat difficult when no X-ray or other complementary spectroscopic data, such as EXAFS, resonance Raman or infrared, are available. Furthermore some of the nitrosylated metalloprotein complexes are diamagnetic (S = 0) or paramagnetic with integer spin (S = 1, 2, etc.), which are EPR-silent with conventional instrumentation. Despite its specificity EPR spectroscopy is therefore much less in general use than other spectroscopic methods, such as resonance Raman or NMR. See chapter 3 for the basic principles of EPR spectroscopy and chapters 4 and 5 for its exemplary application to hemoglobin in vitro and in red blood cells.

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Henry, Y.A. (1997). Utilization of Nitric Oxide as a Paramagnetic Probe of the Molecular Oxygen Binding Site of Metalloenzymes. In: Nitric Oxide Research from Chemistry to Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1185-0_7

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