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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Chapter 16, Problem 2P
If palmitic acid is subjected to complete combustion in a bomb calorimeter, one can calculate a standard free energy of combustion of 9788 kJ/moI. From the ATP yield of palmitate oxidation, what is the
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The complete combustion of palmitate and glucose yields 9781 kJ ∙ mol−1 and 2850 kJ ∙ mol−1 of free energy, respectively. Compare these values to the free energy (as ATP) obtained though catabolism of palmitate and glucose under standard conditions. Which process is more efficient?
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)
Consider 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?
Chapter 16 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 16 - Prob. 1PCh. 16 - If palmitic acid is subjected to complete...Ch. 16 - Calculate the number of ATPs generated by the...Ch. 16 - Prob. 4PCh. 16 - Prob. 5PCh. 16 - Under conditions where ketone bodies are being...Ch. 16 - Prob. 7PCh. 16 - 2-Bromopalmitoyl-CoA inhibits the oxidation of...Ch. 16 - When the identical subunits of chicken liver fatty...Ch. 16 - Prob. 10P
Ch. 16 - Prob. 11PCh. 16 - Prob. 12PCh. 16 - Prob. 13PCh. 16 - Prob. 14PCh. 16 - Prob. 15PCh. 16 - What would be the effect on fatty acid synthesis...Ch. 16 - Prob. 17PCh. 16 - Identify and briefly discuss each mechanism...Ch. 16 - Prob. 19PCh. 16 - Prob. 20PCh. 16 - Prob. 21PCh. 16 - Prob. 22PCh. 16 - Prob. 23PCh. 16 - 24. If mevalonate labeled with 14C in the carboxyl...Ch. 16 - Prob. 25PCh. 16 - Identify a pathway for utilization of the four...Ch. 16 - Prob. 27PCh. 16 - cis-Vaccenate is an 18-carbon unsaturated fatty...Ch. 16 - 29. Briefly describe how cyclic AMP controls...Ch. 16 - Prob. 30PCh. 16 - Prob. 31PCh. 16 - In addition to the pathway described in Figure...Ch. 16 - Prob. 33P
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- Inside 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_forwardA new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?arrow_forwardAcetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.arrow_forward
- If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphatearrow_forwardexplain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/molarrow_forwardWhen 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 = eqarrow_forward
- The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1 kJ/mol. Calculate the equilibrium constant for the reaction. Calculate AG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM. Is the reaction spontaneous under these conditions? HOCH, -20;POCH, H H H H H H ОН Н НО ОН Н H НО ОН H ОН H. ОН Glucose-l-phosphate Glucose-6-phosphatearrow_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] 1.25 mM [oxaloacetate] = 0.290 mM [NAD+] = 430 mM [NADH] : = 170 mM AG : kJ-mol-1 * TOOLS x10arrow_forwardCalculate the standard free energy change (AG) for the transfer of electrons from succinate to ubiquinone: Succinate + ubiquinone O-2.7 kJ/mol O2.7 kJ/mol O-8.7 kJ/mol O 14.7 kJ/mol succinate dehydrogenase relevant half-reactions and standard reduction potentials: fumarate + 2 H* + 2 e succinate ubiquinone + 2H + 2 e -6.0 kJ/mol 11 Fumarate + ubiquinol ubiquinol E = 0.031 V E = 0.045 Varrow_forward
- Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/molarrow_forwardIf the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for sucrose synthesis from glucose + fructose is +5.5 kcal/mole, calculate standard free energy change for the combined reaction of ATP + glucose + fructose g ADP + sucrose + inorganic phosphate. DGo = -12.8 kcal/mole DGo = -1.8 kcal/mole DGo = 0 kcal/mole DGo = +1.8 kcal/mole DGo = +12.8 kcal/molearrow_forwardPhosphocreatine (G0ʹ = -43.1 kJ/mol) has a higher phosphoryl group transfer potential than ATP (G0ʹ = -30.5 kJ/mol). However, under certain physiological conditions, phosphoryl group is transferred from ATP to creatine. Explain this discrepancy. Many biochemical conversions are carried out via multi-step pathways although similar conversions can be done in an organic chemistry lab in fewer steps. Explain why energetically it is reasonable to use multiple steps in biochemical conversions. What are isozymes? Humans contain several isozymes of hexokinase. Why does the body need several isozymes of hexokinase? 1,3-bisphosphoglycerate is used to produce ATP. Which of the two phosphates of 1,3- bisphosphoglycerate is transferred to ADP to make ATP. Explain why it is this specific phosphate and not the other one. Triose phosphate isomerase is a diffusion-controlled enzyme. What reaction is catalyzed by this enzyme (structures of molecules not needed)? Explain why…arrow_forward
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