1. The following data were recorded for the enzyme-catalyzed reaction S→ P. [S] in M 6.25 x 10-6 7.50 x 10-6 1.00 x 104 1.00 x 10³ 1.00 x 102 -2 a) Estimate Vmax and Km without generating graph (b) What would y be at [S] =2.5 x 10¹5 M. V umole/min (c) What would y be at [S] = 5 x 105 M. 15 56.25 60 74.9 75 (d) What would y be at [S] = 5 x 105 M if the enzyme concentration were doubled?

1. The following data were recorded for the enzyme-catalyzed reaction S→ P. [S] in M 6.25 x 10-6 7.50 x 10-6 1.00 x 104 1.00 x 10³ 1.00 x 102 -2 a) Estimate Vmax and Km without generating graph (b) What would y be at [S] =2.5 x 10¹5 M. V umole/min (c) What would y be at [S] = 5 x 105 M. 15 56.25 60 74.9 75 (d) What would y be at [S] = 5 x 105 M if the enzyme concentration were doubled?

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

(267) (268) 57 5 La Ce 138.905 140.116 89 90 Ac Th (227) 232.038 Increases 2. According to the collision theory, what 3 circumstances are needed for CH₁₂O, & O₂ to react? Beacting Substances must Collide, must Collide with enough energy. and must collide with the comet orientation 3. What is the activation energy for a chemical reaction? The Limont of free enering that must be added to go from the mangy fel of the Acts 1. For the Table below, use the collision theory to explain. The following equation applies to of the transition State. statements with an asterisk. *C.H12O6 (1 +6026H0 m+ 6CO2 Change in condition Increasing the temperature Increasing the concentration of CH12O6 Decreasing the concentration of 0₂ Increase the surface area by chewing up food in your mouth Decreasing the temperature Increasing the pressure in the container Increasing the volume of the container the reaction occurs in Using a catalyst (like salivary amylase) Does this increase or decrease the rate of…
3. (а) A laboratory manager performed an experiment to investigate the hydrolysis of 2-chlorooctane at different temperatures. The following results were obtained: Temperature (°C) Rate constant, k, (s1) | 1.06 x 10-5 | 3.19 x 10-4 | 9.86 x 104 | 2.92 x 10-3 25 35 45 Using a graphical method, calculate pre-exponential factor k value at 50 °C (ii) (ii)
6. Five reaction mixtures containing equal concentrations of an enzyme are made up to the substrate concentrations [S] indicated in the table below and the initial rates of the reaction (V) are measured. The experiment is repeated with an enzyme inhibitor I present at 0.22 mM in each reaction mixture. (a) Determine Km for the substrate and K, for the inhibitor. (b) Can you say anything about the type of the inhibitor? [S], mM V (µmol/min) (no I) V (µmol/min) (+ 0.22 mM I) 0.1 28 17 0.15 36 23 0.2 43 29 0.5 65 50 0.75 74 61
The enzyme catalase catalyzes the decomposition of hydrogen peroxide: 2 H2O2 ++ 2 H20 + O2 The turnover number (kea) for catalase is 40,000,000 sec-1. The Km of catalase for its substrate H,O, is 0.11 M. (i) In an experiment using 3 nanomole/mL of catalase, what is Vmax? (ii) What is the catalytic efficiency of catalase?
(b) The reaction between H2O2 and lodide; H,0, + 21 + 2H*→ 2H,0 + 12 Proceeds by two parallel mechanism and led to a rate laws, k, [H,0][I] and = k, [H,0][][#*] %3D dt dt The change in observed rate constants with ionic strength for both the mechanisms is given in the following table. k (M's) 0.69 k2 (M's') Sr. no. Ionic strength (1) 19.0 0.00 0.0207 0.66 15.0 3 0.0525 0.67 12.0 4 0.0925 0.68 11.3 0.69 0.1575 0.2025 9.7 0.71 9.2 With the help of this data and corresponding plots, comment on which mechanism between these two would follow Primary salt effect more prominently. rhich tyne of complex mechanism T-jump
The Eºcell = 0.135 V for the reaction 31₂(s) + 5Cr₂O7²-(aq) + 34H*(aq) ? 6103¯ (aq) + 10Cr³+ (aq) + 17H₂O What is Ecell if [Cr₂O72] = 0.027 M, [H+] = 0.21 M, [103] = 0.00028 M, and [Cr³+] = 0.0030 M?
The Arrhenius equation shows the relationship between the rate constant k and the temperature T in kelvins and is typically written as k = Ae-E/RT where R is the gas constant (8.314 J/mol K), A is a constant called the frequency factor, and Da is the activation energy for the reaction. However, a more practical form of this equation IS In = (1-12) Ea R which is mathmatically equivalent to In Ea F (1/2 R T₂ k2 T1 where ki and k2 are the rate constants for a single reaction at two different absolute temperatures (T₁ and T₂). ▼ Part A The activation energy of a certain reaction is 42.1 kJ/mol. At 20 °C, the rate constant is 0.0150s¹. At what temperature in degrees Celsius would this reaction go twice as fast? Express your answer with the appropriate units. T₂ = Submit Part B Value k₂ = Request Answer Submit Given that the initial rate constant is 0.0150s¹ at an initial temperature of 20 °C, what would the rate constant be at a temperature of 200. °C for the same reaction described in Part…
(ii) At elevated temperatures, nitrogen dioxide decomposes to nitric oxide and molecular oxygen: 2NO2(g) – → 2NO(g) + O2(g) The change in concentration of NO2 with time at 300 °C is given below: t (s) 100 200 300 400 500 [NO2]/103 (mol dm-3) 8.0 5.6 4.3 3.5 2.9 2.5 By appropriate plotting of the data and use of this graph: (a) verify that this reaction is second order with respect to NO2; (b) determine the rate constant for this reaction.
In a study of the conversion of methyl isonitrile to acetonitrile in the gas phase at 250 °CCH3NC(g)CH3CN(g)the concentration of CH3NC was followed as a function of time.It was found that a graph of ln[CH3NC] versus time in seconds gave a straight line with a slope of -4.38×10-3 s-1 and a y-intercept of -2.83 . Based on this plot, the reaction is ______ order in CH3NC and the half life for the reaction is _______ seconds.
For an enzyme -catalyzed reaction, KM=10.0 mmol dm-3, vmax=0.250 mmol dm²³ s-'; [E]o= 2.3 x 10-6 mmol dm-3. Calculate the catalytic efficiency (=kb/KM) of the enzyme. 0.920 dm³ mol-l s-1 3.1 x 107 dm³ mol-1 s-1 1.1 x107 dm³ mol-l s-1 0.250 dm³ mol-l s-1
(3) 13. For the following questions, use the following diagrams. Uncatalyzed Reaction Catalyzed Reaction 400 400 300 300 reactants reactants 200 200 100 100 products products Reaction coordinate Reaction coordinate (1) (a) What is the value of the forward activation energy of the uncatalyzed reaction? (1) (b) What is the value of the reverse activation energy of the catalyzed reaction? (1) (c) What is the overall enthalpy (AH) of the forward reaction? Potential energy (kJ) Potential energy (kJ)
(iii) Given that the following data (Table 1) was obtained for the reaction: C2H5NH2 + C,H5COCH2B → C6COCH,NH2C,H† + Br¯(g) Temp/K 295 310 320 k/ mol- dm³ s 2.2 x 104 7.5 x 104 1.5 x 10-3 Table 1 Using a graphical method, calculate the activation energy and pre-exponential factor.