In a mutant human hemoglobin, a mutation in the β chain abolishes binding of 2,3-bisphosphoglycerate (BPG) to the tetramer. How will this mutation influence the ability of this hemoglobin to give up oxygen at the peripheral tissues? Explain, briefly.
2,3-bisphosphoglycerate (BPG) decreases the affinity of hemoglobin to oxygen, usually at the seas level the Hemoglobin releases only 40% of the oxygen it carries to the tissues, but in hypoxic conditions, the hemoglobin has to release more oxygen to the cells, this is achieved by the action of 2,3-bisphosphoglycerate (BPG), it decreases the affinity of hemoglobin to the oxygen so that more oxygen can be released by the hemoglobin to the cells.
so the mutant human hemoglobin, a mutation in the β chain abolishes binding of 2,3-bisphosphoglycerate (BPG) to the tetramer cannot deliver oxygen to cells in hypoxic ( low oxygen conditions) conditions, for example at high altitudes so so those individuals with the mutation cannot survive in low oxygen concentrations.
In a normal human hemoglobin tetramer, the binding of 2,3-bisphosphoglycerate (BPG) is essential for its function in oxygen transport. BPG binds to the central cavity of the hemoglobin tetramer, where it stabilizes the tense (T) state of hemoglobin. This stabilization facilitates the release of oxygen from the hemoglobin molecules at the peripheral tissues where oxygen concentration is lower.
In the case of the mutant human hemoglobin with a mutation in the β chain that abolishes BPG binding, the ability of hemoglobin to give up oxygen at the peripheral tissues will be impaired. Without BPG, the hemoglobin tetramer will have a higher affinity for oxygen, favoring the relaxed (R) state. This means that the oxygen molecules will bind more tightly to the hemoglobin in the lungs, making it more difficult for hemoglobin to release oxygen at the peripheral tissues.
As a result, the mutant hemoglobin will have a reduced ability to unload oxygen where it is needed most, leading to impaired oxygen delivery to the peripheral tissues. This condition could result in less efficient oxygen supply to organs and tissues, potentially causing various health issues, particularly in situations of increased oxygen demand, such as during physical exertion or at high altitudes.
In a mutant human hemoglobin, a mutation in the β chain abolishes binding of 2,3-bisphosphoglycerate (BPG)...
2) We discussed in class how the molecule 2,3-bisphosphoglycerate (BPG) is an inhibitor of hemoglobin (Hb). Answer the following questions about BPG and its regulation of oxygen binding: a) Would BPG have any effect on myoglobin’s ability to bind or release oxygen? If so, describe how BPG would affect myoglobin. If not, why? b) Based on the observation that BPG binds preferentially to partially deoxygenated Hb, briefly explain (1-2 sentences) where BPG is most likely to be most effective on...
H146 of the β -chain of normal adult hemoglobin ends up in close proximity to D94 on the same chain when oxygen is delivered to the tissues. In hemoglobin Hiroshima H146 on the β -chain has been changed to a D through mutation. a) What effect does this mutation have on oxygen binding by hemoglobin Hiroshima, compared to normal hemoglobin? Explain. b) What effect does this mutation have on the Bohr Effect of this mutant hemoglobin? Explain.
How does BPG, or 2,3-biphophoglycerate produce the shift in the oxygen bunding curves shown? (BPG works to effect the binding of oxygen to hemoglobin) Circle the correct choice. a) BPG binds to the R state of hemoglobin tetramer. b) BPG binds to the T state of hemoglobin tetramer. c) BPG binds to the heme group, which blocks access to the oxygen d) BPG oxidizes the iron (II) in the heme group to the iron (III), preventing oxygen from binding. 1.0...
Bisphosphoglycerate (BPG) is a byproduct of glycolysis. It can bind to the deoxy state of hemoglobin but not the oxy state. Complete the sentence to explain how you expect BPG to shift the Hb-oxygen binding equilibrium. Addition of BPG will _______ because the system needs to compensate for _______ in _________ due to BPG.
Explain how pH, carbon dioxide, and 2,3-BPG promote the release of oxygen from hemoglobin. Why is it important to favor the release but not the binding of oxygen to hemoglobin?
Question 31 6 pts 16) Some patients with erythrocytosis (excess Red Blood Cells) have a mutation that converts a Lysine to Alanine at residue 82 in the beta-subunit of hemoglobin. This particular Lysine normally protrudes in the central cavity of deoxyhemoglobin, where it participates in binding 2,3,-bisphosphoglycerate (BPG). What effect would you predict this mutation will have on a) the affinity of hemoglobin for BPG and for b) the affinity of hemoglobin for Oxygen in patients with erythrocytosis? Briefly explain...
The mutation in hemoglobin at β82Lys→Asp results in lowered O2-binding affinity compared to normal hemoglobin. β82 is one of the residues that lines the 2,3-BPG binding site (see the figure above; β82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, suggest a rationale for the observed reduction in O2-binding affinity. Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each...
1. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (azy), whereas maternal erythrocytes contain HbA (022). Consider the oxygen saturation curve shown below and answer the questions that follow: a) Which hemoglobin has a higher affinity for oxygen? Explain how you made that interpretation. +BPG 0.5 -BPG b) What is the physiological significance of the different 02 affinities? 8 10 4 6 po, kPa) 2. In the context of O, binding...
In the mutant hemoglobin known as HB Providence, an asparagine residue in the B-chain replaces Lys-82. In the normal hemoglobin, Lys-82 projects in the cental cavity of the hemoglobin molecule. Predict the effect of the Lys-Asn mutation of the affinity of allosteric modifiers (relative to normal Hb e.g HbA) and describe the effect the mutation would have on the function (oxygen binding) og HB Providence.
Regarding the effects of the affinity of hemoglobin when 2,3-biphosphoglycerate (BPG) is regulating, analyze the biochemical mechanisms that occur to cause the catch and release of oxygen in this manner. Which of the following structural changes occur when deoxyhemoglobin binds to oxygen? Choose the two correct answers and briefly explain why the other two are incorrect: 1.) The proximal histidine (His F8) moves helix F towards the planar heme. 2.) The heme releases CO2 from the other subunits. 3.) A...