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What are the significances of the plateau and the steep portions of the O2-Hb dissociation curve?
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- What Is the P/O Ratio for Mitochondrial OxidativePhosphorylation?What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.Outline the principal events and outcomes of the Krebs cycle.
- Is fadh2 oxidized or reduced?Studies of oxygen transport in pregnant mammals have shown 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 γ and two β subunits (γ2β2), 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 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 hemoglobin? How can the above information be used to explain the different O2 affinities of…Compared to adult Hb (HbA), fetal Hb (HbF) has one less histidine in the central cavity where BPG binds. What is the consequence of this difference in the P50 value? a The P50 value of HbF approaches zero torr at high O2 partial pressures. b The P50 value of HbF approaches 100 torr at high O2 partial pressures. c HbA has a smaller P50 value compared to HbF d HbF and HbA have the same P50 value. e HbF has a smaller P50 value compared to HbA
- From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.What oxidizes fadh2?Inorganic compounds of metallic mercury are presumed from metabolic studies to distribute uniformly after inhalation or ingestion with 8% going to the liver and 92% to the total body. Biological clearance of mercury in each of these tissues occurs by two compartments, 95% with a biological half-life of 40 days and the remaining 5% with a biological half-life of 10,000 days. For an intake of 1 MBq of 203Hg (Tr= 46.61 d). Determine the following 1. Total number of transformations in the Liver. 2. Total number of transformations in the total body.