Abstract
The determination of the X-ray crystal structure of erythrocruorine from Chironomus thummi shows that its tertiary structure is very similar to that of sperm whale myoglobin. Significant differences were, however, observed in the neighbourhood of the haem group. Seven phenylalanines give the haem pocket of erythrocruorine an aromatic character. The distal amino acid residue closest to the haem iron is the unpolar isoleucine E 11 instead of the polar histidine E 7 in myoglobin. In Spite of these differences the oxygen affinity curves of crystallisable Chironomus thummi erythrocruorine and vertebrate myoglobin are virtually identical.
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