Which 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 t switch from T to R states When fully bound to oxygen, AG(R-state)
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- In 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.what is main difference between myoglobin and hemogloin and in what situations/circumstancees are each used and why?The hemoglobin in mammalian blood is usually thought ofsimply as increasing the amount of O2 that can be carried by eachliter of blood. However, in a lecture on hemoglobin, a respiratoryphysiologist made the following statement: “The presence ofhemoglobin in the blood also makes possible the rapid uptakeof O2 by the blood as it flows through the lungs.” Explain thelecturer’s point.
- Blood in our body changes color as a function of its oxygenation state. Given the spectral data below, calculate the absorbance of red light (600 nm) of fully oxygenated and deoxygenated blood. Using this data, determine what percentage of red light would go through a sample of blood that is 50% oxygenated. Assume the patient has a hemoglobin concentration of 10 mM and pathlength of 1 cm.Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobinMyoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.
- Which are not allosteric effects that occur in hemoglobin? Are used by H* Involve binding away from the heme group Increase the Hill coefficient nH Reduce the affinity of heme for O2 Are used by DPGIn sickle cell disease: O poor oxygen binding causes deformation of red blood cells a mutation in the B-chain of hemoglobin causes hemoglobin to polymerize into fibres that distort red blood cells. O the oxygen binding curve of hemoglobin must be shifted to the left hemoglobin is no longer able to bind oxygen myoglobin is not longer able to bind BPG.Which of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at different
- Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?Carbon monoxide (CO) is a colorless, odorless gas produced during combustion of fuels (for example, by car engines and furnaces). The following graph depicts an oxygen dissociation curve in the absence and presence of varying amounts of carbon monoxide. Based on these results, in the presence of 20% CO, when PO2 is 90mmHg you should expect each hemoglobin molecule to have _____ molecule(s) of O2 bound a) 1 b) 2 c) 3 d) 4“The binding of oxygen to hemoglobin exhibits positive cooperativity.” Explain briefly