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A Change In Hemoglobin's Structure Can Disturb Hemoglobin Function

2297 words - 9 pages

A Change in Hemoglobin's Structure Can Disturb Hemoglobin Function

Abstract:
The fact that a molecule?s structure determines its function can be seen through
the oxygen transporter protein, hemoglobin. Hemoglobin can take two forms, oxy state
and deoxy state, and each performs a distinct function for the hemoglobin. In a normal
hemoglobin, the oxygen binds to a heme group during the oxy state and releases oxygen
during the deoxy state. However, when hemoglobin is mutated like in sickle cell anemia,
in which the amino acid glumatic acid is substituted with valine in the sixth position of
beta subunit; the hemoglobin will not function correctly in the deoxy state. This will lead
the hemoglobin to take a sickle shape that will eventually cause sickle cell anemia.
Imagine doing an internship in the emergency department of the hospital,
suddenly, a five year old athlete comes to the ER that is having hard time breathing. The
results from the tests that were done on the athlete show that he could not become like his
idol, Michel Jordan, in basketball because he has sickle cell anemia. During the talk with
one of the doctors that you were working with, you discover that sickle cell anemia is a
hereditary disease that occurs due to the deficiency of the red blood cells. This is caused
by a genetic mutation in the hemoglobin, an oxygen carrier protein, in which one amino
acid is changed to another. This mutation in the structure of the hemoglobin disturbs the
proteins? normal function and eventually leads to sickle cell anemia. Have you wondered
how this small change in the structure of hemoglobin can cause sickle cell anemia, and
3
stop the athlete from playing basketball? Well, this is one of the main topics that will be
explored in this essay.
As how oxygen is vital for an organism?s survival, similarly, hemoglobin is
important for an organism because it is an oxygen carrier protein that transports oxygen
throughout the body. Hemoglobin was one of the first two proteins whose three
dimensional structure was figured through the x-ray method (1). Hemoglobin is found in
the red blood cells in two forms: deoxy, without oxygen and oxy, with oxygen. Like
many proteins, hemoglobin?s function is dependent on its structure, and if there is a slight
change to its structure, as there is in sickle cell anemia, hemoglobin will not function the
same.
As a tetramer, hemoglobin is made up of four globular proteins subunits: two
alpha globins (2?) and two beta globins (2 ?) that are
each arranged in alpha helix structure. Each of the four
globular
Proteins subunits have non-protein heme group. Heme
group consists of a charged iron ion, Fe2+, that is in the
Figure 2 : ( A) Pyrrole ring: (B), Porphrin
ring (3)
Figure 1: Structure of Heme
group (2)
Figure 2: Structure of hemoglobin (3)
4
center of porphyrin ring, to form four pyrrole rings. The three-dimensional structure of
the hemoglobin is a pair of similar ?? dimmers (two...

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