Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 3P
The decomposition of crystalline N2O5
a. Calculate
b. Why is the entropy change so favorable for this reaction?
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Direct methanol fuel cells (DMFCS) have shown some promise as a viable option for providing "green" energy to small
electrical devices. Calculate E° for the reaction that takes place in DMFCS:
CH3OH(I) + 3/2 02(g) → CO2(g) + 2 H20(1)
Use the following values.
AG°H,0(1) = -237 kJ/mol
AG°O2(g)
= 0 kJ/mol
AG°CO2(9)
= -394 kJ/mol
AG°CH3OH(I)
= -166 kJ/mol.
E° =
V
Calculate the concentration of CuS in a solution in which [H3O+] is held constant at 2.0×10-4 M. (Cite the source of your thermodynamic constants)
At 298 K the standard enthalpy of combustion of sucrose is −5797 kJ mol−1 and the standard Gibbs energy of the reaction is −6333 kJ mol−1. Estimate the additional non-expansion work that may be obtained by raising the temperature to blood temperature, 37 °C.
Chapter 3 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 3 - Prob. 1PCh. 3 - Given the following reactions and their...Ch. 3 - The decomposition of crystalline N2O5...Ch. 3 - The oxidation of glucose to CO2 and water is a...Ch. 3 - Prob. 5PCh. 3 - In another key reaction in glycolysis,...Ch. 3 - Assume that some protein molecule, in its folded...Ch. 3 - When a hydrophobic substance like a hydrocarbon is...Ch. 3 - It is observed that as temperature is increased,...Ch. 3 - Suppose a reaction has Ho and So values...
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Undergoing moderate activity, an average person...Ch. 3 - The major difference between a protein molecule in...Ch. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Consider the degradation of glucose to pyruvate by...Ch. 3 - a. Consider the malate dehydrogenase reaction,...Ch. 3 - Bovine ribonuclease folds with Ho = -280 kJmol-1...
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- If the Gibbs free energy change for the reaction; Succinate + FAD →Fumarate + FADH2 is -40KJ/mol at 37° C. Calculate the ratio of FAD: FADH2 in this condition, if [Succinate]=0.75M and [Fumarate]=0.5M at this condition. Half reaction Standard reduction potential (in volts) Fumarate + 2H + 2 e →Succinate 0.031 FAD+2H+ + 2e →FADH2 -0.219arrow_forwardCalculate the standard free energy change (ΔG°′) for the following reaction: ½ O2 + FADH2 → H2O + FADarrow_forwardFor a particular reaction, AH° = −16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change very little with temperature, at what temperature does the reaction change from nonspontaneous to spontaneous in the forward direction? OT= Is the reaction in the forward direction spontaneous at temperatures greater than or less than the calculated temperature? less than greater than Karrow_forward
- Use the following thermodynamic information to calculate ASn for the combustion of rxn acetylene, C,H,. C2H2(g) + 3 02(9) → 2 CO2(9) + 2 H2O(g) J AS rxn mol K (R) J Substance S° mol K C,H,() 201 0,9) 205 Co,(G) 214 H,O(g) 70.0arrow_forwardThe oxidation of glucose to CO2 and water is a major source of energy in aerobic organisms. It is a reaction favored mainly by a large negative enthalpy change. C6H12O6(s) + 6O2(g) →6CO2(g) + 6H2O(l) ∆H° = -2816 kJ/mol ∆S ° = +181 J/mol . K (a) At 37 °C, what is the value for ∆G°? (b) In the overall reaction of aerobic metabolism of glucose, 32 moles of ATP are produced from ADP for every mole of glucose oxidized. Calculate the standard state free energy change for the overall reaction when glucose oxidation is coupled to the formation of ATP at 37 °C. (c) What is the efficiency of the process in terms of the percentage of the available free energy change captured in ATP?arrow_forwardInside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistryarrow_forward
- Calculate the standard free energy change for the following reaction: 3-PG + ATP 1,3-BPG + ADP ---> Given the following standard free energies of hydrolysis: ATP = - 31 kJ/mol 1,3-BPG = - 49.6 kJ/mol 18.6 kJ/mol 80.6 kJ/mol -80.6 kJ/mol 18.6 kJ/molarrow_forwardGlucose 1-phosphate is converted into fructose 6-phosphate in two successive reactions. Reaction 1: Glucose 1-phosphate → glucose 6-phosphate AG'° = -7.3 kJ/mol Reaction 2: Glucose 6-phosphate → fructose 6-phosphate AGʻ° = +1.7 kJ/mol Using the values given, calculate the standard free-energy change, AGʻ°, ,for the sum of the two reactions: sum > Sum: Glucose 1-phosphate → fructose 6-phosphate AG'°, kJ/mol sum Calculate the equilibrium constant, K', eq > for the sum of the two reactions. K'e eq IIarrow_forwardThe following data were obtained for a reaction that catalyzed by an enzyme: Initial concentration of 0.141 0.109 0.077 0.040 0.028 0.020 0.016 the enzyme [S], mol L- Relative velocity, V 22.0 20.5 19.0 12.5 9.0 7.0 6.0 For this reaction, the rate is found experimentally to follow the Michaelis-Menten equation: Vmax[S] Vo = Км+[S] (1) Transform the above equation into a straight-line equation. By plotting a suitable graph, determine the Michaelis constant (KM) and the maximal velocity (Vmax) for the above reaction. Determine the Vmax value when [S] = KM.arrow_forward
- Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021arrow_forwardConsider the following reaction:ATP → AMP + 2 PiCalculate the equilibrium constant (Keq) given the following ΔG°′ values:ATP → AMP + PPi (−32.2 kJ/mol)PPi → 2Pi (−33.5 kJ/mol)arrow_forward[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remainingarrow_forward
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