Percent saturation (%) 90 80 70 60 50 40 30 20 10 0 0 20 40 60 80 100 mm Hg 0 4 8 12 kPa Partial pressure of O$_{2}$ in blood The figure shown shows that a reduction in O$_{2}$ affinity impairs O$_{2}$unloading less than it enhances loading. enhances O$_{2}$unloading less than it impairs loading. impairs O$_{2}$unloading more than it enhances loading.
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Step 1: The figure shows a graph with the x-axis representing the partial pressure of O2 in blood (mm Hg or kPa) and the y-axis representing the percent saturation of hemoglobin with O2. Show more…
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Below are two figures showing the binding site of O2 on hemoglobin and the plot of the binding behavior of O2 for hemoglobin. Hemoglobin can also bind the allosteric modifier bisphosphoglycerate (BPG) at a different location and change its conformation upon binding. This conformational change is also reflected in the shape change of the sigmoidal binding curve. Iron atom O2 loaded in lungs O2 unloaded in tissues Heme group Polypeptide chain Tissues Lungs 1.0 0.8 0.6 20 40 60 80 PO2 (torr) 100 At increased levels of BPG, which direction would you expect the binding curves of oxygen to shift? How does BPG affect the total amount of O2 that can bind? How does BPG affect the affinity of O2 binding to hemoglobin? Does BPG increase or decrease the KD of oxygen binding? Would you expect the BPG levels of someone living at high altitudes to be higher or lower?
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5. Carbon monoxide (CO) binds to free heme molecules more than 20,000 times better than does O2 (that is, the Kd or P50 for CO binding to free heme is more than 20,000 times lower than that for O2), but it binds only about 200 times better than O2 when the heme is bound in myoglobin. Explain the reduction of CO affinity for heme in the context of the protein.
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What effect will the following changes in hemoglobin affinity have on O2? Explain. An increase in partial CO2 pressure in the lungs from 3 kPa to 6 kPa. A decrease in BPG levels from 9 mM to 4 mM. An increase in blood pH from 7.1 to 7.4.
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