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Wgu Biochemistry Task 3

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WGU Biochemistry Task 3
There are several differences between the oxygenated and deoxygenated states of hemoglobin. One difference can be seen in the conformational state of the hemoglobin protein. When oxygenated, the protein takes on the T (tense) state; and when deoxygenated, the protein takes on the R (relaxed) state (Hudon-Miller, 2012b). Another difference arises when oxygen binds to the hemoglobin, resulting in a change in the shape of the protein. In the deoxygenated state, the heme group forms a domed shape; and in the oxygenated state, the heme group takes on a planar shape (Hudon-Miller, 2012b).

The relationship between pH and the ability of hemoglobin to bind and release oxygen is referred to as the Bohr Effect. The blood’s pH level is greatly influenced by the carbon dioxide that is produced by most of the body’s cells during the citric cycle (Hudon-Miller, 2012d). Greater CO2 concentration lowers the blood’s pH level, making it more acidic. In turn, lower CO2 concentration increases the blood’s pH level, making it more basic. Since the lungs function involves breathing in oxygen and blowing out carbon dioxide, the lungs are absolutely crucial in maintaining the pH balance that the blood requires (Hudon-Miller, 2012d). While in the lungs, the hemoglobin becomes saturated with oxygen and slowly delivers it to the body’s tissues as it travels through the bloodstream. At the same time, the hemoglobin is also picking up the carbon dioxide that is produce by the cells so that it can get back to the lungs and be expelled from the body (Hudon-Miller, 2012d). Therefore, hemoglobin has a higher affinity for oxygen in the lungs, where the blood has the most basic pH level because the CO2 has been expelled. In turn, hemoglobin has a lower affinity for oxygen in the body’s tissues, where the blood has the most acidic pH level due to the high CO2…...

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