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Hemoglobin Oxygen Affinity Analysis

This document summarizes sample problems and answers from a lecture on hemoglobin and oxygen binding. It discusses that llama hemoglobin has a lower oxygen affinity than human hemoglobin to release more oxygen in tissues. It also explains that aspartate 94 interacts electrostatically with histidine 146 in deoxyhemoglobin, stabilizing the interaction and increasing the pKa of histidine. Finally, it shows that the mutant hemoglobin Hb Ohio decreases the stability of this interaction, resulting in an oxygen binding curve that is shifted to the right of normal hemoglobin.

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5 views1 page

Hemoglobin Oxygen Affinity Analysis

This document summarizes sample problems and answers from a lecture on hemoglobin and oxygen binding. It discusses that llama hemoglobin has a lower oxygen affinity than human hemoglobin to release more oxygen in tissues. It also explains that aspartate 94 interacts electrostatically with histidine 146 in deoxyhemoglobin, stabilizing the interaction and increasing the pKa of histidine. Finally, it shows that the mutant hemoglobin Hb Ohio decreases the stability of this interaction, resulting in an oxygen binding curve that is shifted to the right of normal hemoglobin.

Uploaded by

sonicdragon
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

BIOSC

1000

Lecture 7 Sample Problem Answers


1. Would you expect the hemoglobin in a llama, a hoofed mammal native to the Andes of
South America, to have a higher or lower oxygen affinity than human hemoglobin?
You might expect it to be higher to compensate for the lower pO2 in the atmosphere but
actually, the affinity is lower. A lower affinity allows a greater proportion of the O2
bound by the hemoglobin to be released at tissue pO2.
2. The side chain of Asp 94 on the chain of hemoglobin is near the imidazole ring of His
146 in the deoxy form of hemoglobin but not the oxy form.
a. What kind of interaction would you expect to occur between Asp 94 and His 146
in deoxyhemoglobin?
Given that aspartate contains a carboxylic acid side chain and that the histidine
imidazole can be protonated at physiologic pH, an electrostatic interaction would
be expected.
b. Aspartate 94 increases the pKa of histidine 146, what does this tell you about the
interaction of asp 94 and his 146?
An increased pKa translates to needing a higher pH before the imidazole becomes
deprotonated. The effect stabilizes the electrostatic interaction.
3. In the mutant hemoglobin Hb Ohio (142 AlaAsp), the amino acid substitution
decreases the stability of the 146 His-94 Asp interaction. Draw the oxygen binding
curves for HbA and Hb Ohio to show the effect of the decreased stability of the 146
His-94 Asp interaction on O2 binding?
1.0
HbOhio
Y
HbA
0.5

20
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100
pO2, torr

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