6. The rate law for the overall reaction2 N2O5 (g) → 4 NO2 (g) + O2 (g)is Rate = k[N½Os].a. Consider this mechanism:%3Di. N2O5 (g) → NO3 (g) + NO2 (g)ii. NO2 (g) + N2O5 (g) → 3 NO2 (g) + O2 (g) [slow]iii. NO3 (g) + O (g) → NO2 (g) + O2 (g)Is this reaction mechanism consistent with the rate law? Why or Why not?[fast][fast]b. If the reaction mechanism is not consistent with the rate law, how would it needto change to become consistent?c. List potential reaction intermediates present in this mechanism.d. Draw a reaction energy diagram for this mechanism including any modificationsyou've made in a-c.

A reaction mechanism can be defined haste sequence of elementary steps by which a chemical reaction…

Answered: 6. The rate law for the overall…

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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3. (a) In Bakers yeast there are two variants of cytochrome c, a heme containing protein of 108 amino acid residues that catalyzes electron transfer reactions in mitochondria. The two forms of cyto- chrome c known as iso-1 and iso-2 cytochrome c differ in 17 of the 108 amino acids. The content of proton dissociable side chains for the two cytochromes c is given in the table below: Side chain pka iso-1 cytochrome c Ziso-1 iso-2 cytochrome c 12.5 3 4.0 4 8.0 4.0 6.0 10.0 9.0 7.0 4.0 Arginine Aspartate Cysteine Glutamate Histidine Lysine Tyrosine -NH3Ⓡ -COOH 1 4 4 16 5 1 1 What is the overall electrostatic charge on each cytochrome at pH 8? (b) To the right is a diagram of the chemical groups in carboxymethyl-cellulose and DEAE-cellulose that are used for ion exchange chromatography to purify proteins. At pH 8 which chromatographic resin has to be used to separate iso-1-cytochrome c from iso-2-cytochrome c from a lysate of yeast cells? If the proteins are separated by application of a…
7. Representative values of Vm and ApH for the inner mitochondrial membrane and the thylakoid membrane at 25°C are provided in the table. Vm Арн 1.0 pmf Inner mitochondrial 0.166 V 0.2251 membrane Thylakoid membrane O,1483 0.03 V B) What is the value of AG for the thermodynamically feasible (“downhill") movement of 1 mole of H across the inner mitochondrial membrane?
11. Chambers and coworkers have reported [NAD*] and [NADH] concentrations in yeast mitochondria as 20 mM and 0.3 mM, respectively. Consider the Malate Dehydrogenase reaction below: Malate + NAD* → Oxaloacetate + NADH + H* AG° = +29.7 kJ/mol If Malate concentration in yeast mitochondria is 0.4 mM what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 37°C? А. 7.14 х 105 В. 2.04 х 104 С. 8.17 х 106 D. 5.45 x 108 Е. 2.63 х 107 F. 4.69 x 108 G. 4.90 X107 Н. 3.13 х 106 I. 5.05 х 106
4. Anammox bacteria are known to obtain energy from the anaerobic autotrophic oxidation of one mole of NH4+ with N02- to form one mole of N2. (1) Develop an electron equivalent energy reaction for the anammox organisms. (2) Calculate ΔGr (kJ/1nol) for this reaction. (3) Calculate fs° for the anammox autotrophic reaction, assuming ε =0.4, N02- is the N source, inorganic carbon is the carbon source and Y is in g VSS/g N.
Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the above
4
Please show all your work please, thank you! Sorry, this question has many parts. The reaction O3(g)+O(g)→2O2(g), occurs via the following mechanism:Step 1: Cl(g)+ O3(g)→ClO(g)+O2(g); Ea=85 kJ/molStep 2: ClO(g)+ O(g)⇌Cl(g)+O2(g); Ea=10 kJ/mol a. Given the proposed mechanism above, identify any catalysts and any intermediates in this reaction. Be sure to distinguish between the two types of species in your answer. b. Using the proposed mechanism, derive a rate law. *Hint: use the activation energies to determine the slower step. Show all of your work. c. This mechanism was verified by kinetic measurements of the rate of depletion of ozone. How is the rate of change of oxygen gas concentration related to the rate of change of ozone concentration?
3. Show the calculation of (1) the expected grams of alum (KAI(SO4)2 12 H2O) formed from the reaction of 1.4 grams of aluminum metal and then show the calculation of (2) the % yield if the actual yield of alum is 21.31 grams. Overall reaction is shown below: 2 Al + 2 KOH + 10 H2O + 4 H2SO4 →2 KAI(SO4)2 12 H2O + 3 H2(g)T
5. Given the following information tables, determine in which cell type cleavage of the terminal phosphate from ADP yields the greatest actual change in free energy. (Please work in kJ/mol.) TABLE 13-6 Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds and Acetyl-CoA (a Thioester) TABLE 13-5 Total Concentrations of Adenine Nucleotides, Inorganic Phosphate, and Phosphocreatine in Some Cells AG (kJimol) (kcalimol) Concentration (MM) Phosphoenolpyruvate 1,3-Bisphosphoglycerate (+3-phosphoglycerate + P) Phosphocreatine -61.9 -14.8 ATP ADP AMP P, PCr Rat hepatocyte Rat myocyte 49.3 -11.8 3.38 1.32 0.29 4.8 -43.0 -103 8.05 0.93 0.04 8.05 28 ADP (+ AMP + P) -32.8 -7.8 -7.3 Rat neuron 2.59 0.73 0.06 2.72 4.7 ATP (+ ADP + P) Location of -30.5 Human erythrocyte 225 0.25 0.02 1.65 ATP (+ AMP • PP) AMP (+ adenosine P) cleavage is important! 45.6 -10.9 E. coli cell 7.90 1.04 0.82 7.9 -14.2 -34 For erythrocytes the concentrations are those of the cytosol (human erythrocytes lack a…
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
3. The reaction shown below is catalyzed along the pathway of glycolysis by an enzyme with the active site architecture shown. A. The enzyme has two Mg2+ ions, a lysine general base (deprotonated) and a glutamate general acid. In the box below, draw a plausible mechanism for this reaction, which has two formal steps with one intermediate between them (hint: one step uses the general acid and the other uses the general base.) O +(87 -00 11 R-00 00 00 + H₂O OH O Mg2+ Mg2+ Lys (general base) NH₂ OH Glu (general acid) enzyme active site
38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? 유 CH3-C-CH₂-C-S-ACP A B OH 유 CH3-C-CH₂-C-5-ACP → A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor B

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