Calculate the amount of energy a cell could get from methanogenesis (using H2 as an electron donor and CO2 as an acceptor to make CH4) compared to NADH oxidation using oxygen as an electron acceptor. (Remember, the energy values shown in the table will have the opposite +/- sign for the reverse reaction) a) Which one gives more energy? b) How much more?
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Calculate the amount of energy a cell could get from methanogenesis (using H2 as an electron donor and CO2 as an acceptor to make CH4) compared to NADH oxidation using oxygen as an electron acceptor. (Remember, the energy values shown in the table will have the opposite +/- sign for the reverse reaction)
a) Which one gives more energy?
b) How much more?
Step by step
Solved in 4 steps
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH <=> Lactate + NADH+H+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential
- Standard redox potentials Eo' for some common compounds in biochemistry: Eo' (Volt) + 0,81 +0,42 + 0,25 12 O₂ + 2 H+ + 2 e NO3 + 2 H+ + 2 e 2 cyt c (ox) + 2 e 2 cyt b (ox) + 2 e Pyruvate + 2 H+ + 2 e* NAD + 2 H+ + 2 e Acétoacétate + 2 H+ + 2 e (2) acétoacétate + NADH + H+ H₂O NO₂ + H₂O 2 cyt c (red) 2 cyt b (red) Lactate (3) 2 cyt c (ox) + 2 cyt b (red) NADH + H+ B-hydroxybutyrate + 0,08 - 0,19 With the help of the above table, determine the spontaneous direction of the following reactions in the standard conditions. Justify your answers by calculating the Gibbs (free) energy of reaction in each case. (1) pyruvate + ß-hydroxybutyrate -0,32 - 0,35 lactate + acétoacétate B-hydroxybutyrate + NAD+ 2 cyt c (red) + 2 cyt b (ox)Recall that beta-hydroxybutyrate is oxidized by the enzyme beta-hydroxybutyrate dehydrogenase withsimultaneous reduction of NAD+ to NADH. How might this affect the reduction potential at Complex I in theelectron transport chain? (Note: you will need to use the form of the Nernst equation that uses non-standardconditions.)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
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H2O -----> R-OH + HO-P-O3-2Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?A dialyzed pigeon liver extract will catalyze the conversion of acetyl-CoAto palmitate and CoASH if supplied with Mg2+, NADPH, ATP, HCO3-, andcitrate.(a) If H14CO3– is supplied, what compounds will become labeled (permanently or transiently) during the course of the reaction? In whatcompounds will 14C accumulate?(b) Explain the role of citrate in this reaction.
- One 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)(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 torrThe O2-consumption curve of a dilute, well-buff ered suspension of mito chondria containing an excess of ADP and Pi takes the following form: Sketch the curves obtained when (a) amytal is added at time t = 1 and (b) amytal is added at t = 1 and succinate is added at t = 2.