Myoglobin

 
Myoglobin is the simplest type of oxygen carrying molecule in vertebrates. It consists of a single polypeptide chain bound to a heme group. The example shown on the left is sperm whale myoglobin. It shows the heme group edge on (gray) bound to a molecule of oxygen (red balls in the middle of the heme group on the right). The other oxygens, left and top, are part of the heme molecule.

The oxygen is bound to the iron atom at the center of the heme group. In the absence of oxygen this iron atom interacts with the side chains of two histidine residues in the myoglobin polypeptide chain. When oxygen binds it forms a bridge between one of the histidine residues (His-64) and the iron atom in the heme group.

Although the oxygen molecule is tightly bound in this configuration it is still capable of being released under the right conditions. Those conditions can be found inside cells that have become depleted in oxygen. Myoglobin is usually found in muscle cells in vertebrates where it plays a role in storing oxygen. The structure of myoglobin was determined by John Kendrew [Nobel Laureates].

Myoglobin is a member of a large family of globins. They include hemoglobin and similar oxygen carrying molecules in bacteria, plants, and other animals. The myoglobins have evolved from ancestral globins to specialize in oxygen storage inside cells.

©Laurence A. Moran and Pearson Prentice Hall 2007