2. A. Using standard reduction potentials from your textbook, calculate the standard free energy change if FADH; was used to reduce O; to water. B. If AG' for the formation of ATP from ADP and Pi is +12 kcal/mol in the mitochondria, how many ATP could theoretically be produced by the reduction of O2 by FADH: (use your value calculated in A)? What is the actual yield (approximately) of ATP from the reduction of O; by FADH; in mitochondrial electron transport driven ATP synthesis?
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- 1. A cell in an active catabolic steady state state needs to maintain A. a high cytosolic (ATP/ADP) and a high cytosolic (NADH/NAD+) ratio. B. a high cytosolic (ATP/ADP) and a low cytosolic (NADH/NAD+) ratio. C. a low cytosolic (ATP/ADP) and a low cytosolic (NADH/NAD+) ratio. D. a low cytosolic (ATP/ADP) and a high cytosolic (NADH/NAD+) ratio.The standard free energy variation of the ATP hydrolysis reaction is ΔGº’ = -30.5 kJ / mol ATP + H2O ⇄ ADP + Pi In red blood cells, when the concentration of Pi is 1.6 mM, the real change in energy free is ΔG = - 50'2 kJ / mol. a) Calculate under these conditions what is the ratio [ATP] / [ADP] in the red blood cells. b) Determine the equilibrium constant K 'of the reaction outlined above. c) If the ADP concentration were 0.2mM, what would be the effective concentration of ATP corresponding to equilibrium.5. a) The cell creates molecules of NADH and FADH2to use in the electron transport chain as they are electron carrier molecules. The electron transfers from these moleculesdrives the movement of what molecule across the mitochondrial membrane?b) What is chemiosmosis?c) How does the cell use chemiosmosis to drive overcome the thermodynamic barrier of bringing phosphates close togehter to create ATP?d) What steps of oxidative phosphorylation are in the cytosol and which are in the mitochondria?e) Cellular respiration can be controlled at the post-translational level. What does this mean, using GLUT as an example? Why is post-translational control of GLUT evolutionarilyadaptive over transcriptional control?f) How does establishment of equillibria of various molecules control metabolic reactions? What are three ways high ATP in the cell control cellular respiration?g) Why are the enzymes controlling the initial steps of various biochemical pathways are targeted by allosteric control?
- 1) When a de-coupler such as 2,4-DNP is added to a respiring mitochondrion, which of the following effects on the process of ETC-OP will be true, which will be false. a) Mitochondria no longer reduce O2 to H2 b) Electrons no longer enter the electron transport chain. c) Activity of Complex V (ATP Synthase) is greatly decreased. d) The P/O ratio for FADH2 becomes larger than the P/O ratio for NADH. e) Protons are no longer pumped from the mitochondrial matrix to the intermembrane space. 2) The rate-limiting step in fatty acid synthesis is: a) condensation of acetyl-CoA and malonyl-CoA. b) formation of acetyl-CoA from acetate. c) formation of malonyl-CoA from malonate and coenzyme A. d) the reaction catalyzed by acetyl-CoA carboxylase.When pure reduced cytochrome c is added to carefully prepared mitochondria along with ADP, Pi, antimycin A, and oxygen, the cytochrome c becomes oxidized, and ATP is formed, with a P/O ratio approaching 1.0.(a) Indicate the probable flow of electrons in this system.(b) Why was antimycin A added?(c) What does this experiment tell you about the location of coupling sitesfor oxidative phosphorylation?(d) Write a balanced equation for the overall reaction (including cyt c oxidation and ATP synthesis).(e) Calculate ΔG°′ for the above reaction, using E′0 values from Table 14.1and a ΔG°′ value for ATP hydrolysis of -32.2 kJ/mol.Assuming that the pH of the IMS is 1.4 units lower than the pH of the matrix, the free energy yield associated with the transport of a proton from the mitochondrial intermembrane space (IMS) to the mitochondrial matrix is △ G of the reaction is 8.310 KJmol-1 What is the minimum number of protons that must enter the mitochondrial membrane from the IMS in order to synthesize one molecule of ATP?
- Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?You are isolating mitochondria from insect cells and incubating in a test tube with 0.005 M FADH2, 0.05 M ADP and 0.05 M Pi. Assuming, these 3 can enter mitochondria at no cost,no glucose/products of glucose metabolism remain in the isolated mitochondria, and oxygen is present. Part 1) If all expected reactions go to completion, how much ATP is expected formed? (0 M)(0.02 M) (0.03 M) (0.05 M) (0.1 M) (0.005 M) (0.01 M) (0.015 M) Part 2) The ratio of FADH2/FAD at completion of all expected reactions would be? (2) (>>2) (0) (1) Part 3) After completion of all expected reactions, ratio of H ion concentration inside vs. outside the mitochondrial inner membrane should be? (<1) (~1) (>1)(0) Please provide brief explanationDCCD (diocyclohexylcarbodiimide) inhibits oxidative phosphorylation when the substrate is mitochondrial NADH. DCCD is a drug that binds to ATP synthase and blocks proton transport through the ion channel. a) Explain what the consequences of DCCD on cellular energy production are. b) Suggest at least one other cellular effect of DCCD and explain this effect.
- 1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?1. The phosphorylation of glucose with HPO42- forms glucose 1-phosphate and water and requires 5.0kcal/mol of energy. a. Write the equation for this reaction. b. This unfavorable reaction can be driven by the hydrolysis of ATP to ADP. Write the equation for the coupled reaction. c. Calculate the energy change for coupled reactionA new ATP-producing protein is discovered that couples ATP production to the oxidation of NADPH by oxidative phosphorylation. Assume that the value of ΔGo for ATP synthesis is 30 kJ•mol−1. If this protein only produces 1 molecule of ATP per reaction that consumes one NADPH: a. How much free energy is wasted, under standard conditions?b. How many more ATP molecules could be created by a perfectly efficient electron transport chain from one NADPH?