Abstract
This chapter focuses on properties of single-chain hemoglobins. The aqueous monomeric hemoglobin of lamprey, pacific hagfish, and worm hemoglobin on equilibration with carbon monoxide show the sigmoid-shaped curve and heme–heme interaction. The Chironomus Hb curves were very steep and the affinity for carbon monoxide was very high in comparison with hagfish and worm hemoglobin. The absorption bands of all hemoglobins show one narrow CO absorption band, except for lamprey hemoglobin. The cooperative effects in proteins and regulatory enzymes were always correlated to the sequential changes in the conformations of subunits. The absorption bands of the monomeric hemoglobins appeared at 1968, 1974, 1972, and 1968 cm−1 instead at 1952 cm−1 as in human hemoglobin. The monomeric hemoglobins must polymerize under the experimental conditions applied, or there must be other phenomena in the monomeric species giving effects similar to the results of cooperativity in the tetrameric hemoglobins.
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