Abstract
The known structures for the tetramers of mammalian and clam hemoglobins provide a point of departure for the modeling of putative dimers of lamprey hemoglobin. The association of subunits is dissimilar for the clam and mammalian tetramers; the superposition of the molecular model for lamprey methemoglobin onto the mammalian and clam tetramers gives five distinct dimers. After energy minimization of the interface regions of the five models, three models afford promising interactions between side chains. One model is analogous to the alpha 1 beta 2 pairing of subunits of mammalian hemoglobins. The other two models are similar to the interfaces between the E and F helices and between the A and B helices of clam hemoglobin. Although the model based on the alpha 1 beta 2 mode of association provides the best explanation of biochemical properties of lamprey hemoglobin, such as the Bohr effect and the dependency of dimer formation on pH, interfaces between the E and F and the A and B helices could be important in the aggregation of monomers of lamprey hemoglobin beyond the level of the dimer.