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Publisher Summary This chapter discusses the isolation and oxygenation reactions of nitrosylmyoglobins. A remarkable aspect of the mammalian nitric oxide (NO) signal transduction system is that heme proteins are involved in both the biosynthesis of NO from arginine and, in the case of soluble guanylyl cyclase, in its detection. The NO is used as a structural mimic for dioxygen, as both ligands bind in a bent manner to the iron; the important practical difference is that NO forms an odd electron complex and is readily detected by electron spin resonance (ESR) spectroscopy. The spectroscopic characterization of heme protein nitrosyls is carried by a diverse set of techniques including resonance Raman spectroscopy, Fourier transform infrared (FTIR) spectroscopy, magnetic circular dichroism (MCD) spectroscopy, and by electronic spectroscopy (UV–Vis). The simplest method to remove excess impurities in the nitrosylmyoglobin (MbNO) solution is to gel filter under anaerobic conditions. A stoichiometric amount of sodium nitrite is added to a pre-gel-filtered anaerobic solution of metmyoglobin (metMb) and is followed by a stiochiometric amount of sodium dithionite. |
