Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 8.2, Problem 2R
Summary Introduction
To review:
Whether the given reaction is exergonic or endergonic and ATP is hydrolyzed or released during the reaction.
Given:
The given reaction is as follows:
Introduction:
The
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When grown anaerobically on glucose, yeast (S. cerevisiae) converts pyruvate to acetaldehyde, then reduces acetaldehyde to
Pethanol using electrons from NADH.
Write the chemical equation for the reaction that reduces acetaldehyde (CH3CHO) to ethanol (CH3CH2OH).
The table provides the standard reduction potential, E', of the relevant half-reactions.
Half-reaction
Acetaldehyde + 2 H+ + 2e¯ → ethanol
NAD+ + 2H+ + 2e¯ → NADH + H+
E'° (V)
-.197
-.320
Calculate the equilibrium constant, K'eq, at 25.0 °C for the reaction that reduces acetaldehyde to ethanol.
K'e
×10
=
eq
What terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.)
it is non-spontaneous and endothermic (because the overall DGo is negative)
it is spontaneous and exothermic (because the overall DGo is negative)
it is non-spontaneous and endothermic (because the overall DGo is positive)
it is spontaneous and exothermic (because the overall DGo is positive)
it is non-spontaneous and exothermic (because the overall DGo is negative)
Balance the following net reaction that occurs during oxidative phosphorylation. Use the smallest whole integers possible for the reaction stoichiometry.
NADH+ FADH₂ + ADP+ 0₂+H+PO, ¹
NAD+FAD+ ATP+
+H₂O
Chapter 8 Solutions
Life: The Science of Biology
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- Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMarrow_forwardConsider a series of experiments in which 32P-labeled inorganic phosphate were introduced to erythrocytes (red blood cells) undergoing glycolysis. Would you expect to see the labeled phosphate in any glycolytic intermediates? If so, which and at what relative concentrations?arrow_forwardThe 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.arrow_forward
- Decylic acid is a saturated fatty acid that occurs naturally in coconut oil and palm kernel oil. Calculate the net ATP yield when decylic acid undergoes complete B oxidation. The formula of decylic acid is shown below: (Given: The oxidation of one NADH yields 2.5 ATP; the oxidation of one FADH2 yields 1.5 ATP; and the oxidation of one acetyl CoA yields 10 ATP.) O 50 ATP O 52 ATP 66 ATP OH O 64 ATParrow_forwardWrite the coupled reaction that would occur spontaneously for the following pairs of molecules under standard condition: Oxaloaxcetate and NAD+arrow_forwardConsider the following phosphoryl group transfer reaction which is the first step in glucose catabolism by glycolysis: Glucose + ATP + Glucose 6-phosphate + ADP The AG for the reaction is -16.7 kJ/mol. (R= 8.314 J/(K. mol) (a) Calculate Keq for the reaction at 25°C (b) What is the ratio of [Glucose 6-phosphate] to [Glucose] if the ratio of [ADP] to [ATP] is 10?arrow_forward
- Shown below are reduction potentials for four half-reactions. Which of the coupled reactions is favorable? (Note that for Cytochrome c you must multiply the reduction potential by 2 for each coupled reaction because only one electron is involved) a) 2 Cytochrome c (Fe3+) + H2O ó 2 Cytochrome c (Fe2+) + O2 b) NADH + Succinate- ó NAD+ + Fumarate- c) Fumarate- + H2O ó Succinate- + O2 d) All of the abovearrow_forwardConsider the following list of phosphorylated compounds with their free energy changes of phosphate hydrolysis: Glucose-1-phosphate (-5.0 kcal/mol), PEP (-14.8 kcal/mole), 1,3-bisphosphoglycerate (-11.8 kcal/mole) and Glucose-6-Phosphate (-3.3 kcal/mol). Given that the free energy change of ATP hydrolysis is -7.3 kcal/mole, which of these molecules be directly synthesized by the transfer of a phospho- group from ATP? 1,3-bisphosphoglycerate Glucose-6-phosphate All of those phosphorylated compounds. PEP Glucose-1-phosphatearrow_forwardThe enzyme glutamine synthetase catalyzes the following reaction: glutamate + ATP + NH3 → glutamine + ADP + phosphate Which of the following statements about this reaction is correct? a. The reaction is endergonic whether or not enzyme is added b. The reaction is only endergonic if enzyme is added c. The reaction is only exergonic if enzyme is added d. The rate of oxygen production will be unaffected e. The reaction is exergonic whether or not enzyme is addedarrow_forward
- With reference to your experimental protocol, why does adding the reaction mix to the “stop” tubes immediately stop the enzymic reaction? A.Stop tubes contain acid molybdate and the high pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 9.0. B.Stop tubes contain acid molybdate and the high pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 6.0. C.Stop tubes contain acid molybdate and the low pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 9.0. D.Stop tubes contain acid molybdate and the low pH of this reagent will denature the alkaline phosphatase, which has an optimal pH of 6.0.arrow_forwardRegarding phosphofructokinase, which of the following statements is true: a. Low [ATP] stimulates the enzyme, but fructose-2,6-bisphosphate inhibits. b. High [ATP] stimulates the enzyme, but fructose-2,6-bisphosphate inhibits. c. The enzyme is more active at low [ATP] than at high, and fructose-2,6-bisphosphate activates the enzyme. d. High [ATP] stimulates the enzyme, and fructose-2,6-bisphosphate activates.arrow_forwardConsider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG" for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.27 mM [oxaloacetate] = 0.210 mM [NAD+] = 320 mM [NADH] = 130 mM AG: -48.5 kJ.mol-¹arrow_forward
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