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- W1968608112 abstract "The kinetics of oxidation of ferro-sulphaemoglobin to ferri-sulphaemoglobin (met-sulphaemoglobin) by ferricyanide have been studied and the ligand binding properties of the product characterized. In contrast to normal haemogiobin, sulphaemoglobin reacts with ferricyanide at a rate of 4.5·103 M−1· s−1 and 1.3·103 M−1·s−1, at pH 6 and 8, in a simple fashion, suggesting equivalence of the α and β chains. The product, met-sulphaemoglobin, shows a high spin-low spin transition with a pK of 7.7 which is associated with the ionization of a single proton. The rate of spin-state change is so fast as to be rate-limited in the oxidation studies. Titration studies show that met-sulphaemoglobin binds the normal ferric haem ligands azide and cyanide both in an essentially non-cooperative manner. The equilibrium constants for azide and cyanide are 9.10-4 M and 3.5.10−4 M, respectively. Kinetic studies show that both ligands combine with the protein in a biphasic manner, the rates of combination varying considerably for both ligands, being 2. l02 M−1·s−1 and 3.3 M−1·s−1 for cyanide and 46 M−1·s−1 and 1.5 M−1·s-−1 for azide. A consideration of the measured dissociation rates of these ligands, taken with the combination rates, suggests that the simple ligand binding processes observed statically arise from a coincidence of the two associated kinetically observed processes. Magnetic circular dichroism spectra appear to substantiate the previous proposal for the structure of the haem of sulphaemoglobin as pseudo-chorin." @default.
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- W1968608112 date "1982-07-01" @default.
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- W1968608112 title "A characterization of ferric sulphaemoglobin" @default.
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- W1968608112 doi "https://doi.org/10.1016/0167-4838(82)90331-4" @default.
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