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Abstract

Native and modified hemoglobin, myoglobin and a and phemoglobin subunits were oxidized by sodium nitrite at pH 6. The experiments were carried out under oxy and deoxy conditions with and without inositol hexaphosphate (IHP). It is shown (a) that under oxy condition low concentration of IHP inhibits the oxidation of native hemoglobin only. However, high concentration of IHP inhibits the oxidation of both myoglobin and modified hemoglobin (digested or 0-93-SH groups blocked). This inhibition is partially counteracted by high oxygen pressure, (b) Under deoxy condition the oxidation rates of all hemeproteins studied are significantly faster than that of native hemoglobin. IHP inhibits the oxidation of all except the myoglobin and hemoglobin subunits. It is concluded that although the IHP inhibitory effect on hemoglobin oxidation by nitrite can be explained by the shift of the R↔T conformational equilibrium towards T conformation, some other structural changes such as alteration in molecular surface charges must occur to account for the effect of IHP on the oxidation of hemeproteins devoid of heme-heme interaction.

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