Please explain QUESTION 4Shown below are reduction potentials for four half-reactions. Which of the coupled reactions isfavorable? (Note that for Cytochrome c you must multiply the reduction potential by 2 for each coupledreaction because only one electron is involved)Half-ReactionE" (V)O2(g) + 2 H* + 2 e → H2O+0.815Cytochrome c (Fe3+) + e → Cytochrome c (Fe2*)+0.22Fumarate + 2 H* + 2e-→ Succinate+0.031NAD* + H* + 2 e→ NADH-0.3152 Cytochrome c (Fe3+) + H20 2 Cytochrome c (Fe2+) + O2NADH + Succinate NAD* + FumarateFumarate + H2O Succinate + O2O All of the above

Several biochemical reactions that occur in a living organism are redox reactions. The standard…

Answered: Shown below are reduction potentials…

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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Question:- 2) oxaloacetate (OAA) occurs as an important intermediate in 2 metabolic processes a) indicate these reaction steps where OAA occurs b) indicate structure for OAA 3) how many reduced equivalents (as electron carrier) are obtained after an oxidation of C16H12O2? describe in detail the structure of these steps.
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
Question 1: ATP synthases contains 3 copies of each of the large subunits (called α and β in the E. coli enzyme). The number of c subunits can vary among different ATP synthases, ranging from 8 to 17. Part a: Briefly explain how this variation in the number of c subunits would affect the energetics of ATP synthesis. For a fixed value of the protonmotive force, how much energy can the gradient provide to drive one revolution of the ATP synthase, in a synthase with 8 c- subunits versus a synthase with 17 c-subunits?
Question 9 - Under anaerobic conditions in the muscle, lactate dehydrogenase catalyzes the reaction converting pyruvate to lactate. What is the metabolic reason for this fermentation reaction? It is necessary to reduce pyruvate before it can be converted to acetyl-CoA and enter the citric acid cycle in muscle. NAD* must be replenished for glycolysis to continue. The reaction creates NADH which can produce additional energy in the electron transport chain. O Lactate is more oxidized than pyruvate.
Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
QUESTION 2An isocitrate dehydrogenase assay was performed on the enzyme sample and found to give an absorbance change at 340nm of 0.5 absorbance units perminute. Given that the molar absorption coefficient (E) is 6220 M-1 cm-1 and the pathlength is 1cm, what is the rate of the enzyme catalysed reaction in umol perminute per mL?
Question:- 1.) If 2 molecules of glucose enters glycolysis, a total of how many carbon dioxide molecules are released after Krebs Cycle including those released during pyruvate processing?
Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Question 1: In some microorganisms, carbon fixation occurs by reversal of the citric acid cycle. This reversal is accomplished in part by the use of a strong reductant (ferredoxin) to drive the alpha-ketoglutarate dehydrogenase reaction in the reductive direction. Part a: ΔG°‘ for reaction as it occurs in the ‘normal’ (oxidative) citric acid cycle is -30.1 kJ/mol. The standard reduction potential for NADH is -0.32 V. In order to drive the reaction in the reverse direction, the reductant (a ferredoxin) must have a lower reduction potential than NADH/NAD+. Remembering that this is a two-electron reduction, and using the numbers given just above, compute the value of the ferredoxin reduction potential that would be needed to make the standard free energy zero (so that the reductive reaction is enegetically just as favorable as the oxidative reaction). Assume that all of the other reactants are the same in the reductive as in the oxidative reaction. Write out the steps in your calculation;…
Question:- 33) Glucose-6-phosphate has different pathways that it can enter in the liver during the fed state. All of the following are possible except OA.) it is oxidized to acetyl CoA for fatty acid biosynthesis O B). it can enter the pathway for glycogen biosynthesis O c.) it is a substrate for glucose-6-phosphatase OD. )it is oxidized in glycolysis to provide energy for the body
Question 29 options: If 6 molecules of acetyl CoA were completely oxidized by the CAC, how many molecules of FADH2 would be produced?

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