Abstract
HUMAN methaemoglobins, M, form a class of variants in which the haems of two of the polypeptide chains contain ferric ions at all times, while the haems of the other two chains contain iron ions in either the ferric or the ferrous state1. Haemoglobin-M Hyde Park (Hb-M HP) belongs to this group of methaemoglobins. It is characterized by a substitution of tyrosine for histidine in position 92 of the β chains2. This is the fifth co-ordination position of iron. Only α-chains can be oxygenated, even though the oxygen affinity and Bohr effect are similar to those in Hb-A3.
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