Abstract
THE effects of organic phosphates such as ATP, 2,3-DPG, and inositol hexaphosphate (IHP) on the properties of reduced haemoglobin have been recognised for several years and have been the subject of intense investigation1–3 Perutz has recently suggested that at least one of these molecules, IHP, may also interact with methaemoglobin4, 5. He concludes on the basis of optical and near infrared difference spectra that at acid pH, IHP should cause methaemoglobin to change conformation from its normal oxyhaemoglobin-like structure to a deoxyhaemoglobin-like structure. Furthermore, he contends that this change in conformation should be accompanied by an increase in the percentage of high-spin iron (III).
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MAUK, A., MAUK, M. & TAKETA, F. Activation of Methaemoglobin Peroxidase by Inositol Hexaphosphate. Nature New Biology 246, 189–190 (1973). https://doi.org/10.1038/newbio246189a0
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DOI: https://doi.org/10.1038/newbio246189a0
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