1. 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

2. Heme

3. The heme group viewed from the side

4. Myoglobin

5. Binding of oxygen to myoglobin

6. Ligand binding to the heme of myoglobin

7. Comparison of the structure of myoglobin and the beta subunit of hemoglobin

8. Hemoglobin is an α2β2 tetramer that changes conformation from a T state to R state upon binding oxygen

9. Oxygen binding by hemoglobin exhibits a sigmoidal shape, indicating cooperative binding of oxygen and a shift from the R to the T state.

10. A Hill plot indicates the degree of cooperativity for oxygen binding to hemoglobin

11. Models for cooperative binding of oxygen to hemoglobin The concerted model versus the sequential model

12. Effect of pH on oxygen binding to hemoglobin

13. Carbon dioxide binds to the amino terminus of each globin chain of hemoglobin

14. Oxygen binding to hemoglobin is regulated by 2,3-bisphosphoglycerate

16. One BPG molecule binds to the hemoglobin tetramer
T state
R state

17. Erythrocyte shape is altered in sickle cell anemia

18. Normal hemoglobin A has a glutamate on the surface In sickle cell anemia the glutamate is replaced by a valine