- Mutations found to increase oxygen affinity to the hemoglobin.
- This causes increased amounts of red blood cells to compensate for less oxygen being released to the tissues. 

Grand Valley State University

There are many diseases associated with mutations in hemoglobin.
- Sickle-cell anemia 
- Polycythemia 
- Cyanosis
- Hemolytic anemia

Mutations in hemoglobin

Voet, D., Voet, J. G., & Pratt, C. W. (2013). Chapter 7: Protein Function: Myoglobin and Hemoglobin, Muscle Contractions, and Antibodies. In Fundamentals of biochemistry: Life at the molecular level (4th ed., pp. 176-216). Hoboken, NJ: Wiley. Retrieved February 21, 2021, from archive.org.

Fundamental of biochemistry: Life of the molecular level 4th edition: Chapter 7

- Hemoglobins are mutated in that they have less affinity for oxygen and are degraded by erythrocytes (red blood cells) 
- Causes a decrease in the red blood cell count and thus decrease oxygen flow to the tissues.


Hemolytic anemia

- Mutations of the oxygen binding site of hemoglobin causing oxidation of Iron II to Iron III 
- The cooperativity of the binding pockets are decreased in hemoglobin. 
- People exhibit a bluish skin because this mutation creates methemoglobin. 


Cyanosis 

Polycythemia 

- Inheritable blood disease 
- Homozygous (or those with both genes) people with hemoglobin S have sickle-cell disease. 
- Heterozygous individuals usually live healthy lives but have lower erythrocyte count.
- The cells form a sickle shape because of one amino acid is mutated (Glu -> Val)
- This amino acid change allows the hemoglobin to bind to other hemoglobin at the binding pocket causing a mass sickle shape of the blood cells. 
- It is difficult for cells to pass through capillaries and deliver oxygen which can cause tissue death. 


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