The formation of ATP by ATP Synthase is part of a coupled reaction, asdiscussed in class. Given the information below and using what you knowabout ATP Synthase and the proton motive force, calculate the overall AGand determine if the coupled reaction is favorable overall. Note that youdo not need to worry about intermediates like we did for the classexample.ADP + Pi → ATP has a AG = 7.3 kcal/mol2 moles of protons traveling back down their gradient across the innermitochondrial membrane has a AG = -10.28 kcal/mol%3DO a. Overall AG = -17.58 kcal/mol, favorable overallO b. Overall AG = -2.98 kcal/mol, favorable overall%3DO c. Overall AG = 2.98 kcal/mol, unfavorable overallO d. Overall AG = 17.58 kcal/mol, favorable overall

Oxidative phosphorylation is the process by which ATP synthesis is coupled to the movement of…

Answered: The formation of ATP by ATP Synthase is…

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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Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
Assume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal places
Balance the following net reaction that occurs during oxidative phosphorylation. Use the smallest whole integers possible for the reaction stoichiometry. NADH+ FADH₂ + ADP+ 0₂+H+PO, ¹ NAD+FAD+ ATP+ +H₂O
Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surely
Inside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistry
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of ΔG′° can be calculated indirectly, however, from theequilibrium constants of two other enzymatic reactions having less favorable equilibrium constants:Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/mol
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
The standard free energy change for ATP hydrolysis is -7.3kcal/mol. The free energy change under typical cellular conditions is about -12kcal/mol. Why is there a difference? O The hydrolysis of ATP must be more difficult in the cellular environment O There is more ATP and less ADP in the cell O The cellular environment is anaerobic so O2 levels are reduced O The enzymes involved in the reaction are trapped in organelles
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG") of ATP = -31 kl/mol; RT = 2.58 kJ/mol) Select one: a. -28 kJ/mol b. -33 kJ/mol C. -42 kJ/mol d. -19 kJ/mol
The standard free energy of hydrolysis of inorganic polyphosphate (polyP) is about −20 kJ/mol for each Pi released. We calculated in Worked Example 13–2 that, in a cell, it takes about 50 kJ/mol of energy to synthesize ATPfrom ADP and Pi. Is it feasible for a cell to use polyphosphate to synthesize ATP from ADP? Explain your answer.

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