Caiman crocodylus hemoglobin. Complete primary structures of alpha and beta chains; phylogenic and regulatory aspects

In some reptiles, the hemoglobin oxygen affinity is lowered by CO2 and not by the usual phosphate cofactors. To understand the molecular mechanism of this regulation, Caiman crocodylus hemoglobin's primary structure has been determined. The alignment of the 141 residues of the alpha chain as well as the 146 of the beta chain were obtained by classical method of sequence analysis and are compared with some mammalian, avian, amphibian, and fish hemoglobin chains. Furthermore, from these sequences, it is possible to explain the non-interaction of phosphorylated cofactors with the caiman deoxyhemoglobin on the basis of mutations of the amino acids responsible for their fixation on the beta chain. Among these residues only lysine beta 82 is unchanged. In addition a site has been proposed for the fixation of HCO3- which involves ionic bonds with serine beta 1 and glutamic acid beta 144 (Perutz et al. (1981) Nature 291, 682-684) (1).