Concept explainers
Consider the degradation of glucose to pyruvate by the glycolytic pathway:
Glucose + 2ADP + 2Pi + 2NAD+
Calculate
17. For part (b) of this problem, use the following reduction potentials, free energies, and nonequilibrium concentrations of reactants and products:
Consider the last two steps in the alcoholic fermentation of glucose by brewer's yeast:
Pyruvate + NADH + 2H+
a. Do you predict that
b. Calculate the nonequilibrium concentration of ethanol in yeast cells, if
pH = 7.4 and 37o C when the reactants and products are at the concentrations given above.
c. How would a drop in pH affect
d. How would an increase in intracellular CO2 levels affect
e. How would an increase in intracellular CO2 levels affect
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Biochemistry: Concepts and Connections (2nd Edition)
- The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.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_forwarda) The following reaction which is catalyzed by aldolase: Fructose-,6-bisphosphate (FBP) + Glyceraldehyde 3-phosphate (GAP) + Dihydroxyacetone phosphate (DHAP) AG for this reaction is 22.8 kJ mol'. In the cell at 37°C, AG for this reaction is -5.9 kJ mol". Determine the ratio [GAP][DHAP]/[FBP]arrow_forward
- The conversion of dihyroxyacetone phosphate to glyceraldehyde 3-phosphate, catalyzed by triose phosphate isomerase, has an equilibrium constant of Keq’ = 0.0475. Calculate the standard free-energy change for this reaction at 25ºC and pH 7.0.arrow_forwardIn a major metabolic pathway involving the monosaccharide glucose, one of the reactions involve the conversion of glucose to glucose-6-phosphate summarized below together with accompanying free energy change: glucose + phosphate = glucose-6-phosphate + H,0 AG = 13.8 kJ · mol-1 (Reaction 1) In cells, the production of G6P (Reaction 1 above) is coupled to a reaction that involves the hydrolysis of ATP to ADP (shown below, Reaction 2) which makes the overall reaction much more favorable to the production of glucose-6-phosphate. ATP + H,O = ADP + phosphate (Reaction 2) Why do you think coupling the production of glucose-6-phosphate to the hydrolysis of ATP makes the overall reaction spontaneous? What can you say about the free energy change accompanying the hydrolysis of ATP (Reaction 2)?arrow_forwardProline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?arrow_forward
- The reactionPyruvate-(aq) + NADH(aq) + H+(aq) → lactate-(aq) + NAD+(aq)where NAD+ is the oxidized form of nicotinamide adenine dinucleotide, occurs in muscle cells deprived of oxygen during strenuous exercise and can lead to cramp. Calculate the biological standard Gibbs energy, ΔrG⊕, for the reaction at 310 K given that the thermodynamic standard reaction Gibbsenergy ΔrGΘ = -66.6 kJ mol-1.arrow_forwardThe equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]arrow_forwardThe standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alaninearrow_forward
- The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.arrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate.Explain this apparent paradox.arrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate. Explain this apparent paradox.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning