Molecular aspects of embryonic hemoglobin function.
In order to provide the appropriate level of oxygen transport to respiring tissues, we need to produce a molecular oxygen transporting system to supplement oxygen diffusion and solubility. This supplementation is provided by hemoglobin. The role of hemoglobin in providing oxygen transport from lung to tissues in the adult is well-documented and functional characteristics of the fetal hemoglobin, which provide placental oxygen exchange, are also well understood. However the characteristics of the three embryonic hemoglobins, which provide oxygen transport during the first three months of gestation, are not well recognized. This review seeks to describe the state of our understanding of the temporal control of the expression of these proteins and the oxygen binding characteristics of the individual protein molecules. The modulation of the oxygen binding properties of these proteins, by the various allosteric effectors, is described and the structural origins of these characteristics are probed.
Brittain
Thomas
T
School of Biological Sciences, The University of Auckland, Auckland, New Zealand. t.brittain@auckland.ac.nz
D000494:Allosteric Regulation; D001665:Binding Sites; D001692:Biological Transport; D004622:Embryo, Mammalian / Q000502:physiology*; D005319:Fetal Hemoglobin / Q000502:physiology*; D006410:Hematopoiesis / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D010100:Oxygen / Q000378:metabolism*; D010108:Oxyhemoglobins / Q000378:metabolism*; D011485:Protein Binding
D010108:Oxyhemoglobins; D005319:Fetal Hemoglobin; D010100:Oxygen