Phosphoenolpyruvate (PEP) is converted to pyruvate by the enzymepyruvate kinase. The standard free energy change (delta Gº') is -31.4kJ/mol. After eating a candy bar, Billy's cellular concentrations are pyruva-= 0.04 mM and PEP = 12 mM. What is the delta G of this reaction at 37 °CO-33.3 kJ/mol+ 6.3 kJ/molO-46.1 kJ/molO-2.4 kJ/molO-16.7 kJ/mol

The standard free energy change (∆Gº') is the amount of energy released in of biochemical reaction…

Answered: Phosphoenolpyruvate (PEP) is converted…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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 biochemistry
The 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 K
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)
The 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?
The glutamate dehydrogenase (GDH) catalyses the following reaction: *H₂N- H CH₂ CH₂ COO™ acide glutamique COO™ Time (min) A340 + NAD+ + H₂O The answer: GDH 2 1 1.760 1.718 [ammonium sulphate] = 0.33 M [NADH] = 0.205 mg.mL-¹ = 2.9.10-4 M [a-ketoglutarate] = 0.07 M [Protein] = 0.05 mg.mL-¹ COO™ CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. 5 3 4 1.675 1.635 1.595 !- Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. CH₂ The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M-¹.cm-¹ COO acide x-cétoglutarique O + NH4+ + NADH + H* 6 1.550…
Acetyl 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.
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?
The 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.
The reaction below occurs in nearly all human cells. It is catalyzed by the enzyme enolase. CO- CO- enolase -OPO3 OPO3 + H20 ČH,OH AGO'=+1.7 kJ/mol CH2 2PGA PEP Under cellular conditions, the AG is -3.3 kJ/mol. Which of the following could account for these changes in cellular AG compared to the standard biological free energy? The concentration of 2PGA is 7 times higher than PEP. The concentration of PEP is 7 times higher than 2PGA Enolase lowers the activation energy of the transition state. The release of water from 2PGA is a form of energy coupling.
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)?
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] )
The ΔG°’ for the aldolase reaction of glycolysis in muscle is +22.8 kJ/mol. Why does the aldolase reaction proceed in the direction of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate during glycolysis?

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Phosphoenolpyruvate (PEP) is converted to pyruvate by the enzyme pyruvate kinase. The standard free energy change (delta Gº') is -31.4 kJ/mol. After eating a candy bar, Billy's cellular concentrations are pyruva = 0.04 mM and PEP = 12 mM. What is the delta G of this reaction at 37 %