HB is a poor transporter of oxygen OHB is an efficient transporter of oxygen HB is an efficient oxygen storage protein HB binds to oxygen tightly in muscles
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- Below is the oxygen saturation curve for myoglobin and hemoglobin at a pH of 7. The p50 for myoglobin is indicated by the dashed lines on the graph. Mb and Hb O2 saturation: pH 7 10 0.8 Myoglobin 0.6 P50 = 0.2 0.4 Hemoglobin 0.2 - 0.0 pO2 [kPa] Which of these molecules (Mb/Hb/neither or both) has cooperativity? [ Select ] What would you expect to happen to the p50 of myoglobin if the pH were decreased to a pH of 4? [ Select ] Fraction saturationWhich of the following statements regarding the transport of oxygen by hemoglobin is correct? Upon binding of oxygen to heme, a shift in the position of the distal His ultimately induces the switch from T to R states When fully bound to oxygen, AG(R-state)Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?Myoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.Select all statements that correctly describe hemoglobin and myoglobin structure. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron. Molecular oxygen binds irreversibly to the Fe(II) atom in heme. Hemoglobin and myoglobin are heterotetramers. The heme prosthetic group is entirely buried within myoglobin. Each iron atom can form six coordination bonds. One of these bonds is formed between iron and oxygen. Each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind one oxygen molecule. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. 0000To demonstrate an understanding of oxyhemoglobin binding, insert a word from the list in each blank to complete the statements. Not all terms will be used. increased A right shift of the oxy-hemoglobin curve signifies a affinity for oxygen. hold acidic A temperature will cause a right shift of the oxy- hemoglobin curve. basic A more pH than normal blood pH will cause a right shift higher of the oxy-hemoglobin curve. As a person exercises, their muscles give off heat which raises the temperature of the blood. This will cause hemoglobin to more oxygen at the cells. lower release decreasedWhich of these occur when hemoglobin releases oxygen? Select all that apply. O Conformation is shifted toward the T-state BPG can bind in the central channel O Fe2+ is at the center of a planar heme groupIn addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.d) Determine which statements apply to hemoglobin, myoglobin, or neither (you can write in the corresponding numbers for each statement, as appropriate) Hemoglobin Myoglobin Neither 1. Oxygen binds irreversibly to this molecule.2. This molecule has greater affinity for oxygen.3. The oxygen dissociation curve is sigmoidal in shape.4. Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.5. The binding pattern for this molecule is considered cooperative.6. This molecule delivers oxygen more efficiently to tissues.7. As oxygen binds to this molecule, the shape of the molecule changes, enhancing further oxygen binding.8. The oxygen dissociation curve is hyperbolic in shape.The following plot (percent of O2 bound versus [02]) shows three possible curves (A, B, C). In this case, "B" represents the normal oxygen transport protein. Suppose the local concentration of H+ increases. How might this be represented on the graph? Percent O₂ bound A OA shift from B to C B [0₂] OH+ concentration has no effect (remains curve B) OA shift from B to ACrocodiles can use virtually 100% of the oxygen in its blood, whereas humans can extract only about 65% of the oxygen in their blood. Crocodile hemoglobin (Hb) binds HCO3, rather than 2,3-bisphosphoglycerate (BPG), when in the T-state. Which of the following best explains why HCO3¯ in the crocodile works better than 2,3-BPG in humans to help the Hb to release more of its bound oxygen? Crocodile Hb binds more oxygen than human Hb, and so the crocodile has more oxygen available than humans do. The [HCO3] varies with the amount of oxygen used, whereas the [BPG] in human erythrocytes is constant regardless of need. Humans require their hemoglobin to be sensitive to [BPG] in order for HbF (fetal Hb) to have a higher affinity for oxygen than maternal Hb. Since crocodile Hb binds HCO3, the HCO3 will not be available to bind to H+ (Bohr protons), and so more oxygen will be released to the tissues. Crocodiles are cold-blooded and so do not need as much oxygen as humans; this is why they can…Explain how the binding of molecular oxygen (O2) to haemoglobin affects the tertiary structures of each monomer. Hence, explain how this influences the quaternary structure of the haemoglobin molecule, and how this helps haemoglobin to transport O2 from the lungs to the muscles.SEE MORE QUESTIONS
