Molecular adaptation of hemoglobin function in mammals.

@article{Poyart1992MolecularAO,
  title={Molecular adaptation of hemoglobin function in mammals.},
  author={Claude Poyart and Henri Wajcman and Jean Kister},
  journal={Respiration physiology},
  year={1992},
  volume={90 1},
  pages={3-17}
}
Vertebrate hemoglobins are tetramers made of two pairs of alpha and beta subunits each containing a hydrophobic pocket where a heme molecule binds tightly and allows for the reversible binding of oxygen. Both tertiary and quaternary structures are ideally suited for the loading and unloading of oxygen necessary for the metabolic requirements of the organisms. Starting from a single ancestor hemoglobin subunit, evolutionary processes have led to heterologous tetramers exhibiting a moderate… CONTINUE READING