oxygen transport by hemoglobin

Hemoglobin (Hb) constitutes a vital link between ambient O2 availability and aerobic metabolism by transporting oxygen (O2) from the respiratory surfaces of the lungs or gills to the O2‐consuming tissues. The amount of O2 available to tissues depends on the blood‐perfusion rate, as well as the arterio‐venous difference in blood O2 contents, which is determined by the respective loading and unloading O2 tensions and Hb‐O2‐affinity. Short‐term adjustments in tissue oxygen delivery in response to decreased O2 supply or increased O2 demand (under exercise, hypoxia at high altitude, cardiovascular disease, and ischemia) are mediated by metabolically induced changes in the red cell levels of allosteric effectors such as protons (H+), carbon dioxide (CO2), organic phosphates, and chloride (Cl−) that modulate Hb‐O2 affinity. The long‐term, genetically coded adaptations in oxygen transport encountered in animals that permanently are subjected to low environmental O2 tensions commonly result from changes in the molecular structure of Hb, notably amino acid exchanges that alter Hb's intrinsic O2 affinity or its sensitivity to allosteric effectors. Structure‐function studies of animal Hbs and human Hb mutants illustrate the different strategies for adjusting Hb‐O2 affinity and optimizing tissue oxygen supply