Abstract
THERE is considerable X-ray evidence that the haem stereochemistry is different in oxy- and deoxyhaemoglobin1–3. This structural change is an important part of the oxygenation process, because it is believed to induce conformational changes in the surrounding protein that are responsible for cooperativity. We have investigated conformational changes in the haem region by measuring polarised absorption spectra on single crystals. Using this technique we have detected changes in porphyrin plane orientation associated with an alteration of the ligand, spin, and oxidation state of the haem iron, factors which influence haem stereochemistry. Our results not only show for the first time that contacts between the porphyrin and amino acid side chains change upon oxygenation, but they are also consistent with the Hoard-Perutz hypothesis on the nature of the stereochemical trigger1–3.
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MAKINEN, M., EATON, W. Optically Detected Conformational Changes in Haemoglobin Single Crystals. Nature 247, 62–64 (1974). https://doi.org/10.1038/247062a0
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DOI: https://doi.org/10.1038/247062a0
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