Question 4Not yetansweredFlag questionQuestion 5Not yetansweredP Flag questionComplete the following statements regarding the Perutz mechanism for oxygen binding byhemoglobin:The Fe(ll) ion of the heme is pulled into the plane of the porphyrin ring in the T-state ofhemoglobin.A network of ion pairs and hydrogen bonds at the subunit interface stabilizes the R-state ofhemoglobin.Which factor contributes to the Bohr effect on oxygen binding to hemoglobin?Select one:O a. oxidation of the heme bound Fe(l) to Fe(lll) upon oxygen bindingO b.c.O d.O e.hydroxyurea disrupts the aß subunit interface and destabilizes the T-statecarbonic anhydrase catalyzes the formation of bicarbonatenitric oxide binds to the a subunit and inhibits oxygen binding to the ß subunitbinding of 2,3-bisphosphoglycerate stabilizes the T-state of hemoglobin aestionHow does myoglobin minimize oxidation of the Fe(II) when the heme binds to oxygen?Select one:a. the distal His E7 forms a hydrogen bond to the bound molecular oxygenO b. the oxygen binding site is buried in the hydrophobic core away from waterO c. the proximal His F8 forms a coordinate bond to Fe(II), which inhibits oxidationO d. nonpolar interactions with residues Val E11 and Phe CD1 limit oxidation by oxygenOe. the heme shifts to a planar structure that traps iron in a +2 oxidation stateClear my choice

Hemoglobin (Hb) is an oxygen transport protein, which is composed of four subunits. Each subunit has…

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 1P: Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under...

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3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?
A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.
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.
he doctor also mentioned a new treatment for Sickle Cell Disease to JJ called Voxelotor (Oxbryta). Voxelotor binds to the a-globin chain and alters the structure of HbS stabilizing it in the R-state (relaxed state). Q7: In the presence of Voxelotor would you expect the affinity of HbS for O2 to increase or decrease? Q8: How would you classify the mechanism of action for Voxelotor? Q9: Voxelotor's structure is shown below. What would you expect the overall charge of the molecule to be in the blood (pH = 7.4) Pyridinium pKa = 2.6 Phenol pKa = 8.3
Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).
The iron in the iron-heme complex of cytochromes: a. goes from Fe3+ to Fe2+ by the loss of one electron b. always remains in the ferrous (Fe2+) state as in hemoglobin c. goes from Fe2+ to Fe3+ by the addition of one electron d. flip-flops between the reduced (Fe2+) and oxidized (Fe3+) states
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?
2.HbF is the predominant hemoglobin of embrions.It has two γ-and two α-subunits(α2γ2).HbF does not bind 2,3-BPG well.What is the affinity of oxygen binding for HbF in compare with HbA?For answer: 1）Explain the function of HbA and the role of 2,3-BPG in the regulation of O2 binding. 2）Draw the oxygen-binding curves of HbA and HbF. 3）Mark the Biology significance of the difference in O2 affinity for HbA and HbF.
a-Why the ATP production by respiratory complex II is less than Complex I? b-Which molecules do work as the mobile carriers in ETC?
Myoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.
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.

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