Calculate the standard free energy change (AG) for the transfer of electrons from succinate to ubiquinone:Succinate + ubiquinoneO-2.7 kJ/molO2.7 kJ/molO-8.7 kJ/molO 14.7 kJ/molsuccinatedehydrogenaserelevant half-reactions and standard reduction potentials:fumarate + 2 H* + 2 esuccinateubiquinone + 2H + 2 e-6.0 kJ/mol11Fumarate + ubiquinolubiquinolE = 0.031 VE = 0.045 V

Biological oxidation-reduction reactions involve the transfer of electrons from one biomolecule,…

Answered: Calculate the standard free energy…

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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Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
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
Certain bacteria can respire in anoxic environments using arsenic (V) as electron acceptor. The relevant unbalance half reactions are: H₂ AsO+H → H¸AsO +H₂O, logK = 10.84, AG = -14.5kca I m I ol-e CH₂O+H₂OH + CO2 (g), logK = 1.2, AG° = -1.63kca — ol-e 1) Balance the two half reactions 2) What is m the overall respiration reaction, standard free energy change \Delta GO 3) Is this process energetically more or less favorable than sulfate reduction? (\Delta GO for the reduction of sulfate to HS- is -5.78 kcal/mol - e-) 4) If [H2AsO4-] = [ H3ASO3] = 0.5 mM and pH = 7, estimate pe of the system
3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATP
Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous
The 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-alanine
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
NOTE: the enzyme-inhibitor complex requires 450 joule/mol to dissociateJOULE/MOL
Proline 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?
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 0.926

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