Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 20, Problem 20P
Imagine that you are working with isolated mitochondria and you manage to double the ratio of protons outside to protons inside. In order to maintain the overall
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What is the free energy change for generating the electrical imbalance of protons in respiring mitochondria in culture, where Δψ is 150 mV? (Express your answer in kJ/mol using 3 significant figures.)
Processes taking place in the mitochondrion convert the chemical potential energy of NADH into the chemical potential energy of ATP. A proton concentration gradient (Δ[H+]) is part of this process. Describe exactly where this gradient is located, and how the gradient is produced. In terms of the gradient, where is the higher [H+] and where is the lower [H+]?
Suppose the concentration of glucose inside a cell is 0.1 mM and the cell issuspended in a glucose solution of 0.01 mM.(a) What would be the free energy change, in kJ/mol, for the transport ofglucose from the medium into the cell? Assume T = 37 °C.(b) What would be the free energy change, in kJ/mol, for the transport ofglucose from the medium into the cell if the intracellular and extracellularconcentrations were 1 mM and 10 mM, respectively?(c) If the processes described in parts (a) and (b) were coupled toATP hydrolysis, how many moles of ATP would have to be hydrolysed,per mole of glucose transported, in order to make each process favorable? (Use the standard free energy change for ATP hydrolysis.)
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- ATP is synthesized from ADP, P, and a proton on the matrix side of the in- ner mitochondrial membrane. We will refer to the matrix side as the "inside" of the inner mitochondrial membrane (IMM). (a) H* transport from the outside of the IMM into the matrix drives this process. The pH inside the matrix is 8.2, and the outside is more acidic by 0.8 pH units. Assuming the IMM membrane potential is 168 mV (inside negative), calculate AG for the transport of 1 mol of H* across the IMM into the matrix at 37 °C: Houtside) Hinside) (b) Assume three mol H* must be translocated to synthesize one mol ATP by coupling of the following reactions: ADP + P, + Hinskde) ATP + H,O(ATP synthesis) 3Hinside)(proton transport) 3Houtside)arrow_forwardIn the situations described below, what is the free energy change if 1 mole of Na+ is transported across a membrane from a region where the concentration is 48 μM to a region where it is 110 mM? (Assume T=37∘C.) In the absence of a membrane potential.arrow_forwardDiscuss 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?arrow_forward
- The standard free energy of hydrolysis of inorganic polyphosphate (polyP) is about −20 kJ/mol for each Pi released. We calculated in Worked Example 13–2 that, in a cell, it takes about 50 kJ/mol of energy to synthesize ATPfrom ADP and Pi. Is it feasible for a cell to use polyphosphate to synthesize ATP from ADP? Explain your answer.arrow_forwardMany bacterial cells contain an ATP dependent H* transporter that pushes H* out of the cells. The ATP dependent H* pump hydrolyzes 1 ATP to ADP + P; each cycle. Assume that these cells maintain a cytosolic concentration of H* at 10 µM and that the exterior concentration is held at 1.50 mM, while have a resting membrane potential of -60.0 mV (defined for transport into the cytosol), and operate at 25 °C. What is the AGT (total free energy of transport) available to conduct work using the established H* gradient? -12.4 kJ/mol -6.6 kJ/mol -23.9 kJ/mol -18.2 kJ/molarrow_forwardGiven a matrix pH of 7.8 and an inner mitochondrial membrane pH of 7.06, calculate the Nernst potential across the IMM in a lizard cell that is 27 degrees C.arrow_forward
- a) (1) Calculate the physiological AG (not AG.) for the reaction: Phosphocreatine + ADP - creatine + ATP Given; Phosphocreatine + H;0 - creatine + Pi ADP + Pi → ATP + H;0 AG.' -43 kJ/mol AG.- +30.5 kJ/mol at 25°C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM. (R = 8.315 JK-' mol-) (ii) Caleulate the free energy change at standard conditions for the following reaction: Acetaldehyde + NADH + H* + Ethanol + NAD* The half- reactions are: Acetaldehyde + 2H + 2e + Ethanol E°- - 0.20V NAD-+ 2H- + 2e ++ NADH + H- E=-0.32V (F= 96.485 kJ/V/mol)arrow_forwardA 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?arrow_forwardYou know that the free energy of ATP hydrolysis depends on the ATP/ADP ratio. Given that under standard conditions DGo = -30.5 kJ/mol, what should be DG of ATP hydrolysis under normal intracellular concentrations? [ATP] = 2.3 mM, [ADP] = 0.25 mM, [Pi] = 1.65 mM What is the energy of ATP hydrolysis in a cell that is ATP-depleted? [ATP] = 0.1 mM, [ADP] = 2.8 mM, [Pi] = 1.65 mMarrow_forward
- Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.arrow_forwardIn active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?arrow_forwardFor each Pi released, the typical free energy of hydrolysis of inorganic polyphosphate (polyP) is about 20 kJ/mol. In Worked Example 13–2, we determined that synthesizing ATP from ADP and Pi requires roughly 50 kJ/mol of energy in a cell. Is it possible for a cell to manufacture ATP from ADP using polyphosphate? Give an explanation for your response.arrow_forward
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