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…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter6: Metabolism

Section: Chapter Questions

Problem 8RQ: Which of the following is the best way to judge the relative activation energies between two given...

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Similar questions

1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)
Which of the following is the best way to judge the relative activation energies between two given chemical reactions? Compare the ?G values between the two reactions Compare their reaction rates Compare their ideal environmental conditions Compare the spontaneity between the two reactions.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
4 How do I convert from DPM to picomoles per milligram of protein (pmol/mg)? I have the specific activity as [3H]-spiperone is 25530 DPM/pmol. is there an equation?
A certain first order reaction has the rate law Rate = k[A] with k=0.0068 sec-1. If the initial concentration of A is 0.75 M, what will be the concentration of A after 1 minute? What is the half-life for this reaction? How much time will it take for 75% of A to react? How much A will be left after the passage of three half-lives? What is the initial rate of the reaction?
1. Show the complete mechanism for the following reaction 2.) What other method or reaction also reduces benzophenone to diphenylmethane generating few pollutants to keep the environment green? Write the complete reaction.
10) The phosphorylation of glucose is an unfavorable reaction, with ΔG°’ = 13.8 kJ/mol. We can couple this to the favorable reaction of ATP hydrolysis to make the overall process favorable. a) Describe how this works. b) If ΔG°’ for ATP hydrolysis = -32.2 kJ/mol, what is the overall ΔG°’ of the reaction?
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
Using Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?

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