Calculate the standard free-energy change, deltaG'o, for the reaction in which acetaldehyde is reduced by the biological electron carrier NADH in the reaction acetaldehyde + NADH + H+ → ethanol + NAD+. Then calculate the actual free-energy change, deltaG, when the acetaldehyde is 1.51 M, the NADH is 1.02 M, the ethanol is 0.13 M and the NAD+ is 0.19 M, at 33.35oC and pH = 7. Give the actual free-energy change in kJ/mol to one decimal place. See Table 13-7b for the E'o values. TABLE 13-7bStandard Reduction Potentials of Some Biologically Important Half-ReactionsHalf-reactionE" (V)Pyruvate- + 2H + 2e- → lactate--0.185Acetaldehyde + 2H* + 2e- → ethanol-0.197FAD + 2H+ + 2e- → FADH2-0.219aGlutathione + 2H* + 2e- → 2 reduced glutathione-0.23S+ 2H* + 2e¯ → H,S-0.243Lipoic acid + 2H* + 2e- → dihydrolipoic acid-0.29NAD+ + H+ + 2e- → NADH-0.320NADP+ + H*+ + 2e- → NADPH-0.324Acetoacetate + 2H* + 2e- → B-hydroxybutyrate-0.346a-Ketoglutarate + CO2 + 2H* + 2e- → isocitrate2H* + 2e → H2 (at pH 7)-0.38-0.414Ferredoxin (Fe3+) + e¯ → ferredoxin (Fe2*)-0.432Source: Data mostly from R. A. Loach, in Handbook of Biochemistry and Molecular Biology, 3rd edn (G. D. Fasman, ed.), Physicaland Chemical Data, Vol. 1, p. 122, CRC Press, 1976.*This is the value for free FAD; FAD bound to a specific flavoprotein (e.g., succinate dehydrogenase) has a different E" that dependson its protein environment.

NADH is used as the biological electron carrier and is used for the reduction of Acetaldehyde in…

Calculate the standard free-energy change, deltaG'o, for the reaction in which acetaldehyde is reduced by the biological electron carrier NADH in the reaction acetaldehyde + NADH + H+ → ethanol + NAD+. Then calculate the actual free-energy change, deltaG, when the acetaldehyde is 1.51 M, the NADH is 1.02 M, the ethanol is 0.13 M and the NAD+ is 0.19 M, at 33.35oC and pH = 7. Give the actual free-energy change in kJ/mol to one decimal place. See Table 13-7b for the E'o values.

Calculate the standard free-energy change, deltaG'o, for the reaction in which acetaldehyde is reduced by the biological electron carrier NADH in the reaction acetaldehyde + NADH + H+ → ethanol + NAD+. Then calculate the actual free-energy change, deltaG, when the acetaldehyde is 1.51 M, the NADH is 1.02 M, the ethanol is 0.13 M and the NAD+ is 0.19 M, at 33.35oC and pH = 7. Give the actual free-energy change in kJ/mol to one decimal place. See Table 13-7b for the E'o values.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter21: Photosynthesis

Section: Chapter Questions

Problem 13P

See similar textbooks

Similar questions

If you were to determine the P/O ratio for oxidation of α-ketoglutarate,you would probably include some malonate in your reaction system. Why?Under these conditions, what P/O ratio would you expect to observe?
The equilibrium constant Kc for the reaction fructose-1,6-diphosphate ⇋ glyceraldehyde-3-phosphate + dihydroxyacetone phosphate is 8.9 x 10-5 M at 250C and the behavior is assumed to be ideal. Calculate the delta G for the process Suppose that we have a mixture that is initially 0.010 M in fructose-1,6-diphosphate and 1.0 x 10-5 M in both glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. What is the delta G
The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
The high phosphoryl transfer potential of 1,3-bisphosphoglycerate is explained by the resonance stability of the product, 3-phosphoglycerate. The same explanation applies to the reaction that generates resonance stabilized pyruvate from phosphoenolpyruvate. Show the resonance structures for both products, 3-phosphoglycerate and pyruvate, and state why the reactant in both reactions is not resonance stabilized.
If you were to determine the P/O ratio for oxidation of a-ketoglutarate, you would probably include some malonate in your reaction system. Why? Under these conditions, what P/O ratio would you expect to observe?
Behenate (C22H44O2) can be obtained by chain elongation from palmitate. How many ATP equivalents are produced in the degradation of behenate to eleven acetyl-CoA?
Looking at the structure of alpha linolenic acid and knowing the electron carriers produced in each round of traditional beta oxidation for saturated fatty acid chains, how many rounds of beta oxidation will have diminished production of electron carriers due to the presence of double bonds?
Assume that the reaction Arabinose +Pi <> Arabinose-6-P has a delta G of +13.0 kJ/mol and the reaction XTP <> XDP + Pi has a delta G of -25.7 kJ/mol. Calculate the delta G for the combined reaction Arabinose + XTP <> Arabinose-6-P + ADP, in kJ/mol to four significant figures.
The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.
5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) and a ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants andproducts is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction. xylulose-5-PCH2OH CH2OPO32−C OHOHHOH sedoheptulose-7-P
The biochemical standard free energy change for the reaction: A → B is −15.0 kJ/mol. What is the equilibrium constant at 25°C and pH 7? What is the free energy change for the reaction A→B at 37°C when [A]=10.0 mM and [B]=0.100 mM? (Give your answer in kJ/mol)
Using Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?