PRESCOTT'S MICROBIO W/PROCTORIO
11th Edition
ISBN: 9781264731060
Author: WILLEY
Publisher: MCG
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Chapter 10.4, Problem 4CC
In general terms, how is ΔG°′ related to ΔE′0? What is the ΔE′0 when electrons flow from the NAD+/NADH redox pair to the Fe3+/Fe2+ redox pair? How does this compare to the ΔE′0 when electrons flow from the Fe3+/Fe2+ conjugate redox pair to the
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Compare the delta ΔG0' values for the oxidation of succinate by NAD+ and by FAD. Use the data given in Table 18.1 to find the E0' of the NAD+-NADH and fumarate-succinate couples, and assume that E0' for the FAD – FADH2 redox couple is nearly 0.05 V. Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase?
An iron-sulfur protein in Complex 3 donates an electron to cytochrome c1. The reduction half-reactions and Eº' values are shown below. a) write the balanced equation for the reaction and calculate the standard free energy change. b) How can you account for the fact that this reaction occurs spontaneously in the cell?
FeS(ox) + e- ---> FeS(red) Eº' = 0.280 V
cyt c1 (Fe3+) + e- ---> cyt c1 (Fe2+) Eº' = 0.215 V
Below are the reduction reactions for oxygen and FAD.
½202 + 2e + 2H+ → H20
E°' = 0.83 V
FAD + 2e + 2H* → FADH2
E" = -0.22 V
What is the potential (E") for the oxidation of FADH by oxygen?
What is the AG®' for the oxidation of FADH, by oxygen?
If we assume that the pumping of protons in conjunction with the oxidation of FADH, requires 120 kJ, what percentage of the energy from FADH oxidation is stored in the proton gradient (think about how many protons are pumped when FADH, transfers electrons to oxygen)?
Chapter 10 Solutions
PRESCOTT'S MICROBIO W/PROCTORIO
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - Prob. 1CCCh. 10.1 - Prob. 2CCCh. 10.1 - Prob. 3CCCh. 10.1 - Prob. 4CCCh. 10.2 - Why is ATP called a high-energy molecule? How is...Ch. 10.2 - Describe the energy cycle and ATPs role in it....Ch. 10.3 - Prob. 1MICh. 10.3 - Prob. 2MICh. 10.4 - Figure 10.6 Electron Movement and Reduction...
Ch. 10.4 - How is the direction of electron flow between...Ch. 10.4 - When electrons flow from the NAD+/NADH conjugate...Ch. 10.4 - Which among the following would be the best...Ch. 10.4 - In general terms, how is G related to E0? What is...Ch. 10.4 - Name and briefly describe the major electron...Ch. 10.6 - Will an enzyme with a relatively high Km have a...Ch. 10.6 - Prob. 2MICh. 10.6 - Prob. 1CCCh. 10.6 - Prob. 2CCCh. 10.6 - How does enzyme activity change with substrate...Ch. 10.6 - What special properties might an enzyme isolated...Ch. 10.6 - What are competitive and noncompetitive...Ch. 10.6 - How are enzymes and ribozymes similar? How do they...Ch. 10.7 - Figure 10.19 Allosteric Regulation. The structure...Ch. 10.7 - Prob. 2MICh. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 3CCCh. 10.7 - Prob. 4CCCh. 10.7 - Prob. 5CCCh. 10 - Prob. 1RCCh. 10 - Prob. 2RCCh. 10 - Prob. 3RCCh. 10 - Examine the structures of macromolecules in...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 3AL
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- The Eo values for the NAD/NADH and Glyceraldehyde-3-phosphate/1,3- Bisphosphoglycerate conjugate redox pairs are -0.32 V and -0.19 V, respectively. Beginning with 1 M concentrations of each reactant and product at pH 7 and 25 C, which statement is TRUE? Glyceraldehyde-3-phosphate would become oxidized; NAD would become reduced. No reaction would occur because all reactants and products are already at their standard concentrations. Glyceraldehyde-3-phosphate would become oxidized; NADH2 would be unchanged because it is a cofactor. Glyceraldehyde-3-phosphate and 1,3-Bisphosphoglycerate would become oxidized; NAD and NADH would become reduced. 1,3-Bisphosphoglycerate would become reduced; NADH would become oxidized.arrow_forwardShown 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_forwardCertain bacteria can respire in anoxic environments using arsenic (V) as electron acceptor. The relevant unbalance half reactions are: H₂ AsO+H → H¸AsO +H₂O, logK = 10.84, AG = -14.5kca I m I ol-e CH₂O+H₂OH + CO2 (g), logK = 1.2, AG° = -1.63kca — ol-e 1) Balance the two half reactions 2) What is m the overall respiration reaction, standard free energy change \Delta GO 3) Is this process energetically more or less favorable than sulfate reduction? (\Delta GO for the reduction of sulfate to HS- is -5.78 kcal/mol - e-) 4) If [H2AsO4-] = [ H3ASO3] = 0.5 mM and pH = 7, estimate pe of the systemarrow_forward
- Under standard conditions, will the following reactions proceed spontaneously as written? (1) Fumarate + NADH + H+ (2) succinate + NAD+ Cyto a (Fe²+) + cyto b (Fe³+) = cyto a (Fe³+) + cyto 6 (Fe²+) barrow_forwardThe succinate dehydrogenase complex couples the oxidation of succinate to the reduction of ubiquinone (Q) according to the following equation. succinate + Q --> fumarate + QH2 Given that E'° for the fumarate/succinate redox pair is + 0.031V and E'° for the Q/QH2 redox pair is + 0.045V, calculate the standard free energy change (AG") for the oxidation of succinate by ubiquinone. 1º = - 1.35 kJ/mol Ag° = - 2.7 kJ/mol OAG° = - 280 kJ/mol OAG° = + 1.35 kJ/mol %3D OAG° = + 2.7 kJ/mol %3Darrow_forwardOne process catalyzed by NADHNADH dehydrogenase is NADH+H^++ubiquinone ↽−−⇀ NAD+ubiquinolNADH+H^++ubiquinone ↽−−⇀ NAD^++ubiquinol The standard reduction potentials for the half‑reactions are given in the table. Oxidant Reductant ?′0 ubiquinone+2H++2e−ubiquinone+2H++2e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)arrow_forward
- (a) Consider the oxidation of malate to oxaloacetate by NAD*: malate + NAD+ → oxaloacetate + NADH + H+ In yeast mitochondria, where the pH = 8.1, this reaction is exergonic only at low oxaloacetate concentrations. Assuming a pH = 8.1, a temperature of 37 °C, and the steady-state concentrations given below, calculate the maximum concentration of oxaloacetate at which the reaction will still be exergonic. malate + NAD*→ oxaloacetate + NADH + H* lactate + NAD →→ pyruvate + NADH + H+ half reaction Pyruvate + 2H+ + 2e → lactate Pyruvate + CO₂ + H + 2e → malate Intracellular steady state concentrations: malate = 410 μM; NAD = 20.0 mM; pyruvate = 3.22 mM; NADH = 290 μM; AG=+29.7 kJ/mol AG¹ = +25.1 kJ/mol E° (V) - 0.190 - 0.330 lactate 1.1 mM CO₂ = 15.5 torrarrow_forwardConsider the typical beta oxidation of linoleic acid (C18:2 ^Δ9, 12): How many ATP are generated in complete oxidation of linoleic acid? How many NADH are generated in complete oxidation of linoleic acid? How many FADH2 are generated in complete oxidation of linoleic acid?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
- In the complete b-oxidation of stearic acid (18:0) How many moles of FADH2 are produced? How many moles of ATP are produced after all NADH are reoxidized in the respiratory chain? How many moles of ATP are produced after all FADH2 are reoxidized in the respiratorychain? How many moles of ATP are produced from the complete oxidation of stearic acid?arrow_forwardChambers and coworkers have reported [NAD+] and [NADH] concentrations in yeast mitochondria as 20 mM and 0.3 mM, respectively. Consider the Malate Dehydrogenase reaction below: Malate + NAD+ → Oxaloacetate + NADH + H+ ∆G0’ = +29.7 kJ/mol If Malate concentration in yeast mitochondria is 0.4 mM what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 370C?arrow_forwardThe standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol Karrow_forward
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