384 Structure and Function of Hemoglobin Q4.4- In addition to O2, another diatomic molecule that can bind to the iron atom in hemoglobin is CO. Explain in biochemical terms why high levels of CO gas are lethal and cite a specific example of accidental death by CO poisoning (where/when/how).
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384
Structure and Function of Hemoglobin
Q4.4- In addition to O2, another diatomic molecule that can bind to the iron atom in hemoglobin is CO. Explain in biochemical terms why high levels of CO gas are lethal and cite a specific example of accidental death by CO poisoning (where/when/how).
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- Comparison of Fetal and Maternal Hemoglobins.Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting oftwo a and two g subunits (α2γ2), whereas maternal erythrocytes contain HbA (α2β2). a)Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. b)What is the physiological significance of the different O2 affinities? c)When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation curves (and consequently the O2affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2affinity of hemoglobin? How can the above information be used…The primary allosteric regulator of hemoglobin oxygen affinity is ( ) and functions by stabilizing the ( ) state of enzyme.54. 2,3-Bisphosphoglycerate: (MARK ALL THAT APPLY) Group of answer choices is absorbed from food binds in the central cavity in the T-form of hemoglobin. is released by the liver into the bloodstream cannot bind in the presence of oxygen preferentially binds to oxygen-bound hemoglobin and stabilizes it.
- Comparison of Fetal and Maternal Hemoglobins Studies of oxygen transport in pregnant mammals show that the O₂-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain a structural variant of hemoglobin, HbF, consisting of two a and two y subunits (a272), whereas maternal erythrocytes contain HbA (α₂ß₂). 1.0 (b) (c) 0 0.5 0 2 HbF +BPG HbA +BPG 4 6 po₂ (kPa) 1 8 10 (a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain. What is the physiological significance of the different O₂ affinities? When all the BPG is carefully removed from samples of HbA and HbF, the measured O₂-saturation curves (and consequently the O₂ affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O₂-saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O₂ affinity of…1.12 At elevated altitudes, the body adapts to the reduced barometric pressure to extract sufficient oxy- gen to permit normal metabolic functions and do work. For example, at an altitude of 3,650 m (close to 12,000 feet above sea level) the barometric pressure drops to 485 mmHg. For an oxygen pressure drop in the lungs of 30 mmHg, determine the oxygen uptake rate for a respiration rate of 20 breaths per minute. Estimate the oxygen saturation in venous blood if the hematocrit rises to 0.60 and the partial pressure of oxygen blood is at a partial pressure equal to 98% of the alveolar level.1.1 ;) The diagram on the right compares the O2 binding prop- 1.0 erties or normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y = fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes %3D 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 F State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)
- Some terms will not be used. The prosthetic group of hemoglobin and myoglobin is The organic ring component of heme is Under normal conditions, the central atom of heme is In the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring system. The central atom has bonds: to nitrogen atoms in the porphyrin, one to a residue, and one to oxygen. Answer Bank Fe3+ three heme serine deoxyhemoglobin four Fe2+ oxyhemoglobin рoгphyrin histidine six cysteine30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environmentsaestion How 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 oxygen O b. the oxygen binding site is buried in the hydrophobic core away from water O c. the proximal His F8 forms a coordinate bond to Fe(II), which inhibits oxidation O d. nonpolar interactions with residues Val E11 and Phe CD1 limit oxidation by oxygen Oe. the heme shifts to a planar structure that traps iron in a +2 oxidation state Clear my choice
- Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H2O -----> R-OH + HO-P-O3-2Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?Allosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformationPentose phosphate pathway and hemolytic anemia. Explain the relationship.