To carefully prepared mitochondria were added succinate, oxidized cytochrome c, ADP,orthophosphate, and sodium cyanide. The overall balanced equation is:succinate + 2 cyt c(ox) + ADP + Pi --> fumarate + 2 cyt c(red) + ATP + H2OThe standard state free energy of this system isO -10.3 kJ/mol42.5 kJ/molO 10.3 kJ/mol-42.5 kJ/mol

Mitochondria are vital cellular organelles of every cell. They're known as the cell's powerhouse…

Answered: To carefully prepared mitochondria were…

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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You are isolating mitochondria from insect cells and incubating in a test tube with 0.005 M FADH2, 0.05 M ADP and 0.05 M Pi. Assuming, these 3 can enter mitochondria at no cost,no glucose/products of glucose metabolism remain in the isolated mitochondria, and oxygen is present. Part 1) If all expected reactions go to completion, how much ATP is expected formed? (0 M)(0.02 M) (0.03 M) (0.05 M) (0.1 M) (0.005 M) (0.01 M) (0.015 M) Part 2) The ratio of FADH2/FAD at completion of all expected reactions would be? (2) (>>2) (0) (1) Part 3) After completion of all expected reactions, ratio of H ion concentration inside vs. outside the mitochondrial inner membrane should be? (<1) (~1) (>1)(0) Please provide brief explanation
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
The cytochromes are heme-containing proteins that function as electron carriers in the mitochondria. Calculate the difference in the reduction potential (AE°') and the change in the standard free energy (AG°) when the electron flow is from the carrier with the lower reduction potential to the higher. cytochrome c₁ (Fe³+) + e¯ = cytochrome c₁ (Fe2+) E°' = 0.22 V cytochrome c (Fe³+) + e¯ = cytochrome c (Fe²+) E°' = 0.254 V Calculate AE°' and AG°'. AE°' = AG°' = V kJ/mol
a newly identified bacterium called Nomore biochem is unable to synthesize ubiquinone. A mobile electron carrier called CXC3 is used as a substitute. From the information provided in the table, calculate delta G' and Keq value at 298K for the redox reaction that occurs in the Nomore Biochem electron transport chain. (constants: R=8.3 J/degree x mol, F= 96.1 kJ/v x mol Half Reactions E' (V) ubiquinone + 2e- + 2H+--> Ubiquinol + H2 0.045 NAD+ + 2e- + 2H+ --> NADH + H+ -0.320 CXC3 + 2e- + 2H+ --> CXC3H2 -0.450 explain the impact that using CXC3 instead of ubiquinone will have on ATP production in the cell. How might the cell adapt to this situation?
What is the ∆G naught' for a phosphoryl transfer from ATP to glycerol? The hydrolysis of α-glycerophosphate to glycerol and inorganic phosphate has a ∆G naught' of -8.37 kj/mol. ATP + H2O <--> ADP + Pi ∆G naught' = -30.5 kj/mol What is the efficiency of this reaction (i.e. what % of the available energy remains in the system after the reaction)? Express your answer as a % of the total amount of energy available in the system. Where does the rest of the energy go?
What terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.) it is non-spontaneous and endothermic (because the overall DGo is negative) it is spontaneous and exothermic (because the overall DGo is negative) it is non-spontaneous and endothermic (because the overall DGo is positive) it is spontaneous and exothermic (because the overall DGo is positive) it is non-spontaneous and exothermic (because the overall DGo is negative)
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.
In the third step of glycolysis, the given reactions are coupled. reaction 1: fructose-6-phosphate + Pi ⟶ fructose-1,6-bisphosphate + H2O (Δ? = −28 kJ/mol) reaction 2: ATP + H2O ⟶ ADP + Pi (Δ? = +13.8 kJ/mol) Calculate the overall ΔG (kJ/mol) for the coupled reaction.
Aconitase catalyzes the conversion of Citrate to Isocitrate in the TCA cycle. The standard free energy change (AG°) for this reaction is +6.7 kJ/mol. The observed free energy change (AG) for the reaction in pig heart mitochondria is +0.8 kJ/mol. The ratio of [isocitrate]/[citrate] in these mitochondria is: Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 10 b. 1 100 0.01 e f 0.33 0.10 h 0.25 i 2
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
Arsenate (AsO³-) closely resembles phosphate in structure and reactivity. However, arsenate esters are unstable and are spontaneously hydrolyzed. If arsenate is added to actively respiring mitochondria, what would be the effect on ATP synthesis? ATP synthesis will decrease because cells require less energy when arsenate is available. ATP synthesis will not be affected because mitochondria are incapable of taking up arsenate. ATP synthesis will stop due to the formation arsenate-ADP anhydrides. ATP synthesis will increase because arsenate anhydride hydrolysis increases ATP turnover. If arsenate is added to actively respiring mitochondria, what would be the most likely effect on the rate of the electron-transport chain? The rate of electron transport will decrease, because arsenate inhibits Complexes I and II. The rate of electron transport will decrease, because arsenate inhibits the citric acid cycle. The rate of electron transport will increase, because arsenate increases the demand…
The hydrolysis of ATP to ADP has a △G°' of -30 kJ/mol. If in an E. coli cell the concentrations of ATP, ADP and inorganic phosphate are 7.90 mM, 1.04 mM and 7.9 mM, respectively, which statement is true about the hydrolysis of ATP in the cell? (Assume a temperature of 298 K. R = 8.315 J/K-mol) A. The formation of ATP from ADP is occurring more rapidly than the hydrolysis. B. The hydrolysis is being allosterically controlled. C. Hydrolysis can proceed spontaneously. D. The hydrolysis is at equilibrium. QUESTION 10 The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21 help with these questions please

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To carefully prepared mitochondria were added succinate, oxidized cytochrome c, ADP, orthophosphate, and sodium cyanide. The overall balanced equation is: succinate + 2 cyt c(ox) + ADP + Pi --> fumarate + 2 cyt c(red) + ATP + H2O The standard state free energy of this system is