Increases the hydrogen ion concentration causing oxyhemoglobin to precipitate
Changes the valence state of iron in hemoglobin
Competitively displaces oxygen from oxyhemoglobin.
Converts myoglobin to carboxyhemoglobin at a rapid rate
Prevents transfer of oxygen across the alveolar membranes
The heme iron of fetal hemoglobin is Fe3+
Fetal hemoglobin binds 2 hemes per subunit
Fetal hemoglobin is monomeric
Fetal hemoglobin forms more salt bridges
Fetal hemoglobin has a lower affinity for 2,3-BPG
Myoglobin undergoes a conformational change that raises its oxygen affinity above that of hemoglobin
2,3BPG dissociates from hemoglobin and binds to myoglobin.
Much more of the dissolved oxygen binds to myoglobin than to hemoglobin.
Hemoglobin dissociates into its subunits
Most of the hemoglobin becomes oxygenated while most of the myoglobin rema ins deoxygenated
Oxygen binds to Fe+3 but not to Fe+2.
Hydrophobic interactions are the primary forces associated with BPG bind ing to hemoglobin
When oxyhemoglobin moves to a more acidic environment, it is more apt to release its oxygen
Carbon dioxide binds to Fe+2 but not to Fe+3 hemoglobin
Carbon monoxide binds to Fe+3 but not to Fe+2 hemoglobin.
Higher than normal levels of methemoglobin reductase
Nonspherocytic hemolytic anemia
Carbon monoxide poisoning
Exposure to an oxidizing drug
Exposure to pentachlorophenol