David L. Nelson and Michael M.

Cox

LEHNINGER
PRINCIPLES OF BIOCHEMISTRY
Sixth Edition

CHAPTER 5
Protein Function

© 2013 W. H. Freeman and Company

Heme
The heme group
viewed from the
side
Myoglobin
Binding of oxygen to myoglobin
Ligand binding to
the heme of
myoglobin
Comparison of the structure of myoglobin and
the beta subunit of hemoglobin
Hemoglobin is an α2β2 tetramer that changes
conformation from a T state to R state upon
binding oxygen
Oxygen binding by hemoglobin exhibits a sigmoidal shape, indicating
cooperative binding of oxygen and a shift from the R to the T state.
A Hill plot indicates the degree of cooperativity for
oxygen binding to hemoglobin
Models for cooperative binding of oxygen to hemoglobin
The concerted model versus the sequential model
Effect of pH on oxygen binding to hemoglobin
Carbon dioxide binds to the amino terminus of
each globin chain of hemoglobin
Oxygen binding to hemoglobin is regulated by
2,3-bisphosphoglycerate
One BPG molecule binds to the hemoglobin tetramer

T state R state
Erythrocyte shape is altered in sickle cell anemia
 Normal hemoglobin A
has a glutamate on the
surface

In sickle cell anemia the

glutamate is replaced
by a valine