Functional adaptations of oxygen-transport proteins

Abstract

Oxygen-transport proteins are multisubunit, circulating molecules that provide an efficient supply of oxygen to metabolically active metazoans. Hemoglobins, hemerythrins and hemocyanins have evolved in both structural and functional diversity and exhibit functional repertoires beyond that of simple, monomeric tissue myoglobins. Their phylogenetic distribution is intriguing, especially with respect to those organisms that express more than one type of oxygen-transport protein. An animal can modify the delivery of oxygen to its tissues by varying the rate of synthesis of these proteins or by selective expression of individual subunits and/or molecules. Changes in levels of allosteric modifiers that affect the protein's oxygenation properties will also modify oxygen delivery; some organisms have more ability than others to control concentrations of modulators. Hemoglobins have assumed functions in addition to oxygen transport, while hemocyanins have diversified through multiple gene duplications and functional specializations. Understanding the mechanisms of regulation of expression, synthesis and modulator levels is a key focus of current investigations.