Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 14, Problem 15P
a. Calculate the standard free energy change as a pair of electrons is transferred from succinate to molecular oxygen in the mitochondrial respiratory chain.
b. Based on your answer in part a, calculate the maximum number of protons that could be pumped out of the matrix into the intermembrane space as these electrons are passed to oxygen. Assume 25o C, ΔpH = 1.4;
c. At which site(s) are these protons pumped?
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Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP.
a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85.
b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol)
The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
a. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.
a) Make a theoretical calculation of how many ATP molecules
can be formed from the breakdown of a molecule of Acetyl-
CoA into carbon dioxide and water. The prerequisite is that the
entire proton gradient across the mitochondrial inner
membrane can be used for ATP production and that the ATP
synthase has 6 c-subunits.
Chapter 14 Solutions
Biochemistry: Concepts and Connections
Ch. 14 - Prob. 1PCh. 14 - When pure reduced cytochrome c is added to...Ch. 14 - Freshly prepared mitochondria were incubated with...Ch. 14 - Prob. 4PCh. 14 - Prob. 5PCh. 14 - Intramitochondrial ATP concentrations are about 5...Ch. 14 - Prob. 7PCh. 14 - Prob. 8PCh. 14 - Years ago there was interest in using uncouplers...Ch. 14 - Prob. 10P
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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_forwardThe catalytic mechanism of an enzyme found in the mitochondrial matrix (pH = 7.8) depends on an active site Lys residue (pKa = 9.5) that acts as a general acid. Mutation of a neighboring residue alters the microenvironment of the Lys side chain so that its pKa shifts from 9.5 to 7.2. Would the mutation cause the reaction rate to increase or decrease? Explain your answer.arrow_forwardAssuming 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?arrow_forward
- ATP is synthesized from ADP, P, and a proton on the matrix side of the inner mitochondrial membrane. We will refer to the matrix side as the "inside" of the Inner Mitochondrial Membrane (the "IMM"). Show your work. (a) H* transport from the outside of the IMM into the matrix drives this process. Assume the pH inside the matrix is 8.00 and the outside is more acidic by 0.60 pH units. Assuming the IMM membrane potential is 165.0 mV (inside negative), calculate AG for the transport of 1 mol of H* across the IMM into the matrix at 37 °C: H* (outside) → H* (inside)arrow_forwardThe proton-motive force is a measure of the potential energy generated across the mitochondrial inner membrane during electron transport. Explain the factors that constitute this potential energy, that will be converted to the chemical energy of ATP by the cell. 2. The function of the Electron Transport Chain (ETC) in eukaryotic cells is to produce a proton gradient across the mitochondrial inner membrane. How many protons are taken up from the matrix and transferred or used at each ETC complex?arrow_forwarda) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) abovearrow_forward
- Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.arrow_forwardAssume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal placesarrow_forwardCalculate how many moles of ATP can be made in standard conditions when 1 mole of protons flow back into the mitochondrial matrix through the ATP synthase. Assume that: i) the matrix pH is 7.8, ii) the cytosolic pH is 7.2, iii)ΔE=0.168 V (inside negative), iv) T=37°C, and v) the standard free energy change for the hydrolysis of 1 mole of ATP is -31.3 kJ/mol.arrow_forward
- a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) abovearrow_forwardConsider the coupled reactions: 1,3-BPG → 3-PG + Pi ΔG°'= -16.3 kcalmolkcalmol ATP → ADP + Pi ΔG°'= -7.3 kcalmolkcalmol Which of the following is TRUE about the total ΔG°’ for the coupled reactions? A. +23.6 kcal/mol; nonspontaneous B. -23.6 kcal/mol; spontaneous C. +9.0 kcal/mol; nonspontaneous D. -9.0 kcal/mol; spontaneousarrow_forwardImagine that in red blood cells (RBCS) the following concentrations were noted for the "adenylate pool": [ATP] = 2000 uM; [ADP] = 270 uM; and [AMP] = 30 uM. ASsume that the pH is 7 and remains constant. a) calculate the Energy change (EC) (to four decimal places for RBCS given the above values. Show work b) If the [ATP] decreases by 5%, calculate the new [ATP], [ADP], and [AMP] given that the concentrations of all three species are "connected" by the adenylate kinase reaction, which is shown below. You will need to use the quadratic equation for this one. show your work. %3| %3D ADP + ADP ATP + AMP Keq = 0.44arrow_forward
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