Hemoglobin Is The Conjugate Molecule Biology Essay


These iron ion can hold up to four molecules of oxygen which is in this way transported in the different parts of body. (Pin S et al., 1982)

n the deoxygenated (T) state, the iron atom becomes non-planar with the rest of the heme group due to its association with a histidine side chain.

While in the Oxygenated state Oxygen binding causes the iron atom in the heme to move such that it becomes planar with the rest of the heme group, which then pulls the histidine, causing a larger scale structural change in the protein.

In the oxygenated state hemoglobin is called oxyhemoglobin and is bright red.

In the reduced state it is called Deoxyhemoglobin and is purple - blue in color. (Michael W King, PhD)

Myoglobin can be regarded as an extremely compact heme protein

It is basically present in cardiac and red skeletal muscles

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Their main function is to store the oxygen and also carry out the transport of oxygen to the mitochondria for oxidative phosphorylation. (Nelson, D. L and Cox, M. M. 2000)

The amount of oxygen which is carried out or released by by the hemoglobin is not only depend upon potential pressure of Oxygen but also on the pH as well.

If the environment is acidic then it make the oxygen to release or dissociates from the hemoglobin.

So we can identify now that small decrease in pH can results in larger unsaturation of Hemoglobin with oxygen as shown in figure. This shift is regarded as Bohr Effect. (Olson et al., 1972).

Myoglobin can be regarded as an extremely compact heme protein

It is basically present in cardiac and red skeletal muscles

Their main function is to store the oxygen and also carry out the transport of oxygen to the mitochondria for oxidative phosphorylation. (Nelson, D. L and Cox, M. M. 2000)

Hemoglobin consists of four protein chains and four heme groups that carry oxygen from the lungs to the tissue cells.

Myoglobin consists of a single protein chain with 153 amino acids and one heme group that stores oxygen in the muscle cells.

Myoglobin has a stronger affinity for oxygen then hemoglobin, which enables the oxygen to shift from one to the other.

Sickle cell anemia is caused by an abnormal type of hemoglobin called hemoglobin S.

Hemoglobin S changes the shape of red blood cells, especially when the cells are exposed to low oxygen levels. The red blood cells become shaped like crescents or sickles.

Sickle cell anemia is a disease passed down through families in reality red blood cells are of disc shaped but in sickle cell anemia the shape of red blood cells form an abnormal crescent shape. (Powars et al., 1991)

Sickle cell disease block the oxygen molecule and does not allow it to move to the different organs of the body as a result these organ start dying without oxygen.

The red blood cells of patients with sickle cell disease are not able to live as long as healthy red blood cells.

As a result, people with this disorder often have low red blood cell counts (anemia), which is why this disease is commonly referred to as sickle cell anemia.

Sickle cell disease is inherited in an autosomal recessive pattern.

Like a child will not inherit the disease unless both parents contribute the defective copy of the gene.

People who inherit one good copy of the gene and one mutated copy are carriers.

They are clinically normal, but can still pass the defective gene to their children. (Lesi et al., 1972)

Doctors suggests that Babies and young children with sickle cell disease should take a daily dose of penicillin in order to avoid potentially deadly infections.

Patients also take folic acid, which helps build new red blood cells.

Doctors advise people with sickle cell disease to get plenty of rest, drink lots of water, and avoid too much physical activity.

Blood transfusions and bone marrow transplant is commonly used for the treatment of sickle cell anemia. (Aldrich and Nagel 1998)

In the United States, African-Americans are most effecting from this disease.

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About 1 out of every 500 African-American babies born in the United States has sickle cell anemia.

Sickle cell disease is also most common among people from Africa, India, the Caribbean, the Middle East, and the Mediterranean. (retrieved from http://www.nlm.nih.gov/medlineplus/sicklecellanemia.html)

Robert I. Weed, Claude F. Reed, and George Berg (1963). "IS HEMOGLOBIN AN ESSENTIAL STRUCTURAL COMPONENT OF HUMAN ERYTHROCYTE MEMBRANES?". J Clin Invest. 42 (4): 581-8.

Perutz MF (November 1960). "Structure of haemoglobin". Brookhaven symposia in biology 13: 165-83

Pin S, Alpert B, Michalowicz A. (Oct 1982). "Oxygen bonding in human hemoglobin and its isolated subunits: A XANES study". FEBS Lett. 147 (1): 106-10.

Michael W King, PhD. "The Medical Biochemistry Page - Hemoglobin". http://themedicalbiochemistrypage.org/hemoglobin-myoglobin.php#hemoglobin. Retrieved 2012-09-13.

Olson, JS; Gibson QH, Nagel RL, Hamilton HB (December 1972). "The ligand-binding properties of hemoglobin Hiroshima ( 2 2 146asp )". The Journal of Biological Chemistry 247 (23): 7485-93

Aldrich TK, Nagel RL. (1998). "Pulmonary Complications of Sickle Cell Disease.". In Reynolds HY, Bone RC, Dantzker DR, George RB, Matthay RA. Pulmonary and Critical Care Medicine (6th ed.). St. Louis: Mosby. pp. 1-10.

Nelson, D. L.; Cox, M. M. (2000). Lehninger Principles of Biochemistry (3rd ed.). New York: Worth Publishers. p. 206.

Powars DR, Elliott-Mills DD, Chan L, et al. (Oct 1991). "Chronic renal failure in sickle cell disease: risk factors, clinical course, and mortality". Ann. Intern. Med. 115 (8): 614-20.

Lesi FE, Bassey EE (July 1972). "Family study in sickle cell disease in Nigeria". J Biosoc Sci 4 (3): 307-13.