Biochemistry Module 3.

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Myoglobin and hemoglobin each have different numbers of subunits and this affects their respective oxygen storage and delivery capabilities. How many subunits do myoglobin and hemoglobin each have? S... elect one: Addition of alters the shape of the iron–heme complex, and therefore its absorption of light as indicated by its color change from dark purple (the color of hemoglobin in venous blood) to brilliant scarlet (the color of hemoglobin in arterial blood). Select one: Oxygen binding alters the structure of an entire hemoglobin tetramer, so the structures of oxyhemoglobin and deoxyhemoglobin are noticeably different. The oxyhemoglobin conformation is specifically referred to as the state, whereas the deoxyhemoglobin conformation is referred to as the state. Select one: Patients with sickle cell anemia have atypical hemoglobin, which will distort the red blood cells into sickle shape during oxygen delivery. The substitution of a hydrophilic amino acid with a amino acid in hemoglobin subunits results in the polymerization of hemoglobin, leading to the sickling of red blood cells. Select one: Hemglobin consists of four proteins subunits. Each subunit contains a heme group that holds an iron atom, which can bind to an oxygen molecule. When binding hemoglobin or myoglobin, CO binds in place of . Select one: Structurally, hemoglobin can bind molecules of oxygen, all of which could potentially be replaced by carbon monoxide. Select one: Carbon monoxide outcompetes oxygen for attachment to the group of hemoglobin where it is permanently, covalently attached. Select one: As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow carbon monoxide to bind faster. This process is called . Select one: Carbon monoxide shifts the Oxygen-Hemoglobin Dissociation Curve to the left, while carbon dioxide shifts this curve to the right. Based on your knowledge of the Bohr Effect, which of the following statements is true? Select one: Carbon dioxide, released by the respiring cells, combines with the water molecules of plasma to form carbonic acid. Carbonic acid increases the H+ ion concentration (low or acidic pH). H+ ions stabilize the deoxy-conformation (T state) of hemoglobin and allow oxygen release and delivery to the tissues. On the other hand, carbon monoxide, which has a very high affinity for hemoglobin than oxygen, binds and maintains hemoglobin in oxy-conformation (R state). Oxy-conformation of HB is amenable to further binding of carbon monoxide and shifts the Oxygen-Hemoglobin Dissociation Curve to the left. Hemoglobin’s cooperative binding behavior is key to its physiological function. The binding of which of the following molecules influences this behavior? Select one: Carbonic anhydrase is an important present in the red blood cells that aids in efficient transportation of carbon dioxide in the form of , from tissues to lungs. Select one: Hemoglobin’s ability to bind or release oxygen depends on the pH of the environment. This behavior is known as the Bohr effect. Considering this, which of the following statements is true? .........................................................................................continued............................................................................ [Show More]

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