Describe how the following allosteric effectors regulated Hemoglobin’s O2 affinity: • CO2 • H+ (pH; Explain the basis for the Bohr Effect) • 2,3-BPG • CO
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Describe how the following allosteric effectors regulated
Hemoglobin’s O2 affinity:
• CO2
• H+ (pH; Explain the basis for the Bohr Effect)
• 2,3-BPG
• CO
Step by step
Solved in 2 steps with 4 images
- Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effectorAfter spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?The primary allosteric regulator of hemoglobin oxygen affinity is ( ) and functions by stabilizing the ( ) state of enzyme.
- What is the Bohr effect? What role does BPG play in hemoglobin function?Considering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of hemoglobin, calculate how many molecules of oxygen one erythrocyte could carry?Which hemoglobin has a higher affinity for O2 at the tissue pO2 of around 4 kPa?
- Describe the effect of 2,3- bisphosphoglycerate on the binding of oxygen by hemoglobin.Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?Correlate the conformational changes to the cooperative behavior of the oxygen-binding ability of hemoglobin
- “The binding of oxygen to hemoglobin exhibits positive cooperativity.” Explain brieflyOxygen has an allosteric interaction with hemoglobin. What are the results of this interaction as oxygen a) binds to and b) is released from hemoglobin?What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.