1. Calculate the overall AG°' (reported up to two decimal places) for the net reaction. kJ/mol 2. Calculate the Keg (reported up to two decimal places and do not use scientific notation) for the net reaction at 298.15K.
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- 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 equilibrium at 298 K. R=8.314 J/K-mol Acetyl-CoA + Oxaloacetate + H20 Citrate + COASH + H* Which one of the following is the correct value for K'eg ifAG" = -32.2 kJ/mol? O 1.11 0.987 1.01 x 10-13 13.0 9.92 x 1012 2480 4.42 x 105 2.27 x 10-6 1.01 -2480 2.56 -13.0 1.08 -0.0130 0.0130 0.926The standard free energy change for this reaction in the direction written is +23.8 kuimol. The tabie shows the concentrations of the three intermediates in the hepatocyte of a mammal. Intermediate Concentration (M) Fructose 1.0-bisphosphate 0.000028 Gyoeraldehyde 3phosphate 0.0000068 Ditydroxyacetone phosphate 0.000032 At body temperature (37 "C). what is the actual free energy change for the reaction (in kimol) ?
- 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 KCalculate 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 VCarbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!
- The formation of acetyl-CoA from acetate is an ATP-driven reaction: Acetate + ATP + CoA Acetyl CoA + AMP + PP₁ Calculate AG" for this reaction given that the AG' for the hydrolysis of acetyl CoA to acetate and CoA is −31.4 kJ mol-¹ (−7.5 kcal mol¯¹) and that the AG°' for hydrolysis of ATP to AMP and PP; is -45.6 kJ mol-¹ (−10.9 kcal mol−¹ ). AG° reaction = AGO! i The PP, formed in the preceding reaction is rapidly hydrolyzed in vivo because of the ubiquity of inorganic pyrophosphatase. The AG" for the hydrolysis of pyrophosphate (PP;) is −19.2 KJ mol-¹ (-4.665 kcal mol-¹). Calculate the AGº' for the overall reaction, including pyrophosphate hydrolysis. reaction with PP, hydrolysis = What effect does the presence of pyrophosphatase have on the formation of acetyl CoA? kJ mol-¹ It does not affect the overall reaction. It brings the overall reaction closer to equilibrium. It makes the overall reaction even more exergonic. It makes the overall reaction even more endergonic. kJ mol-¹ -1You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).explain 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/mol
- A 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?Acetyl-CoA AG" = -7.7 kcal/mol COA Fatty acids Oxaloacetate Citrate AG" = -1.5 kcal/mol Isocitrate Krebs cycle is equilibrium at 25°C with coupled fatty acid biosynthesis. Calculate the free energy of the fatty acid biosynthesis (in kcal/mol), accounting for the concentrations of Oxaloacetate – 0.005 mM; Acetyl-CoA - 0.03 mM; Citrate - 0.001mM and Isocitrate – 0.06 mM.Consider the two half-reactions below and their standard reduction potentials. NAD+ + H+ + 2e → NADH Elo= -0.32 V a-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V (a) What is AE" for the spontaneous redox reaction that is, the reaction that actually occurs under standard biochemical conditions (pH 7)? (b) Which of the following statements are correct under standard biochemical conditions? i. The concentration of H+ is 1.0 M. ii. The reaction NAD+ + Isocitrate → NADH + H+ + a-Ketoglutarate + CO₂ is favor- able. iii. NAD+ accepts electrons from isocitrate. iv. The NAD → NADH reaction actually occurs in reverse. The a-ketoglutarate → isocitrate reaction occurs as written. (c) Calculate AG" for the reaction in (a). (pH 7, 25°C, pressure, 1 atm.) (d) Suppose that the actual conditions are T = 25°C, pH = 7, CO₂ = 1 atm, [a-Ketoglutarate] 10 mM, [NAD+] = 2.5 mM, and [NADH] = 0.5 mM. PAR = 2 mM, [Isocitrate] DE What is the value of AG under those conditions? (Hints: pH 7 is already…