Isomeric Incorporation of the Haem into Monomeric Haemoglobins of Chironomus thummi thummi

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Abstract
13C-NMR studies on 13CO complexes of the components III and IV of the monomeric haemoglobins from the subspecies Chironomus thummi thummi have been carried out in order to confirm the existence of two conformational isomers differing by the isomeric incorporation of the haem group and the extent of the Bohr effect. In addition, the allosteric linkage between the ligand binding site and the Bohr proton binding site in the component IV is described from investigations of various pH-dependent proton resonances including the C-2 proton resonances of the titratable histidines. In comparison to the data obtained for the component III it is assumed that in both conformational isomers of the component IV the allosteric linkage between the distal site of the haem and the main Bohr proton donating group is present. From corresponding NMR investigations of the component I an isomeric incorporation of the haem group into this monomeric haemoglobin seems unlikely. Also, any correlation between the ligand binding site and a titratable group of the protein had not been found in this haemoglobin, in agreement with previous results of other laboratories that a Bohr effect in the component I cannot be detected.