LEHNINGER PRINCIPLES OF BIOCHEMISTRY

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Presentation transcript:

LEHNINGER PRINCIPLES OF BIOCHEMISTRY 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