"Oxygen reversibly binds to the iron (Fe2+) atom within each haem moiety, forming oxyhaemoglobin, following the release of the oxygen it becomes deoxyhaemoglobin. The affinity with which oxygen binds to the haemoglobin is modified by pH (Bohr effect 2), body temperature and the concentration within red cells of a molecule known as 2,3-bisphosphoglycerate (2,3-BPG), dependent - in turn - on the partial pressure of oxygen (pO2) 3,4."
"Carbon monoxide (CO) binds to haemoglobin forming carboxyhaemoglobin (COHb). Carbon monoxide has a stronger affinity than oxygen for haemoglobin, thus displacing the oxygen from the haemoglobin, such that less oxygen is available to the tissues."
Expected headings
"Structure"
"Physiology"
"Related pathology"
"Oxygen reversibly binds to the iron (Fe2+) atom within each haem moiety, forming oxyhaemoglobin, following the release of the oxygen it becomes deoxyhaemoglobin. The affinity with which oxygen binds to the haemoglobin is modified by pH (Bohr effect 2), body temperature and the concentration within red cells of a molecule known as 2,3-bisphosphoglycerate (2,3-BPG), dependent - in turn - on the partial pressure of oxygen (pO2) 3,4."