The O2-binding curve for Hemoglobin (Hb) is sigmoidal because:a O2 binding to Hb increases the binding affinity of Hb for additional O2.b The pH of blood is near the pKa of histidine.c The pH of the bloodstream changes with changes in O2 concentration.d Hb’s O2-binding affinity changes with changes in pH.

Hemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. As this limit is…

Answered: The O2-binding curve for Hemoglobin…

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter8: Blood

Section: Chapter Questions

Problem 3RQ

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One molecule of 2,3-bisphosphoglycerate (BPG) binds to one molecule of haemoglobin (Hb) in a central cavity of the haemoglobin molecule. Is the interaction between BPG and Hb stronger or weaker than it would be if BPG were bound to the surface of the protein instead? Explain your answer.
A mutation in Hb that prevented formation of the tetramer would result in: a A decrease in overall O2 binding affinity but increased O2 transport to muscle. b Increased O2 binding in muscle but decreased binding in lung. c A loss of positive cooperativity and reduced O2 transport efficiency. d All of the above.
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.
A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in a) Not enough information b) Normal binding to oxygen c) Higher than normal binding affinity to oxygen d) Lower than normal binding affinity to oxygen
To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Explain why?
In an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?
A crocodile, which can remain underwater without breathing for up to 1 hour drowns its air-breathing prey, then dines at its leisure. An adaptation that aids the crocodile in doing so is that it can utilize virtually 100% of the O2 in its blood whereas humans, for example, can only extract about 65% of the O2 in their blood. Crocodile Hb does not bind BPG. However, crocodile deoxyHb preferentially binds HCO3-. How does this help the crocodile obtain its dinner? Please help explain why/if this is the answer, thank you! As CO2 concentrations increase so will the concentration of HCO3-. The HCO3- preferentially binds to the crocodile's deoxyhemoglobin, which allosterically prompts the hemoglobin to assume the deoxy conformation and thus release its O2.
Hemoglobin (Hb) is a blood protein that is responsible for transporting oxygen. It can exist in the protonated form as HbH*. The binding of oxygen can be represented by the simplified equation HbH+ + 02 > ABO2 + Ht A. Excessive vomiting may lead to metabolic alkalosis, in which [H2O*] in blood decreases. How does this condition affect the ability of Hb to transport O2? B.Diabetes mellitus may lead to metabolic acidosis, in which [HgO*] in blood How does this condition affect the ability of Hb to transport O?
A mutation in the alpha globin gene that introduced one additional basic amino acid residue in the BPG binding pocket would: (select one) a) Eliminate Hb’s positive cooperativity. b) Decrease Hb’s O2 binding affinity. c) Increase Hb’s O2 binding affinity. d) Increase O2 binding in muscle and decrease it in lungs. e) Decrease O2 binding in muscle and increase it in lungs. f) It would have no effect on the adult form of Hb.
Highly active muscles generate lactic acid by respiration so fast that the blood bassing through the muscle actually experiences a drop in pH from 7.4 to 7.2. Under these conditions, hemoglobin releases about 10% more O2 than it does at pH 7.4. Explain.
Protons influence the binding affinity of oxygen to hemoglobin. Based on the oxygen-transport mechanism of hemoglobin, which of the following is correct? A. The pH value of lung is lower than that of tissue B. Protons compete with oxygen C. Protons will facilitate oxygen release in lung D. Production of lactate during exercise will accelerate oxygen delivery.
) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.

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a		O2 binding to Hb increases the binding affinity of Hb for additional O2.
b		The pH of blood is near the pKa of histidine.
c		The pH of the bloodstream changes with changes in O2 concentration.
d		Hb’s O2-binding affinity changes with changes in pH.