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Spectral differences between the alpha and beta heme groups within human deoxyhemoglobin


, : Spectral differences between the alpha and beta heme groups within human deoxyhemoglobin. Proceedings of the National Academy of Sciences of the United States of America 73(4): 1140-1144

The contributions of the alpha and beta heme groups to the absorbance change that accompanies the aggregation of hemoglobin subunits were measured by comparing the extinction changes produced by n-butyl isocyanide binding to deoxyhemoglobin A with those produced by binding of n-butyl isocyanide to the isolated chains. Almost the entire aggregation absorbance change is associated with the unliganded alpha subunits, which exhibit a 30% increase in molar extinction at 428 nm during tetramer formation. This marked spectral change indicates a substantial perturbation of the electronic properties of the alpha heme groups in going from the high-affinity, isolated chain state to the low-affinity, tetrameric state. The lack of a significant absorbance change as sociated with the beta heme groups implies that the change in reactivity of unliganded beta subunits produced by aggregation is not the result of a change in spin or coordination geometry of the iron atom, but rather involves primarily an alteration in the protein structure near the sixth coordination position.

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Accession: 041408806

PMID: 1063394

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