QUESTION 13 Given the following data for an enzyme kinetics experiment. Determine the value of the Michaelis-Menton constant Km [S]o (HM) v (nmol/min) 0.20 1.43 0.26 1.72 0.33 2.07 1.00 3.60 A. 62.3 μm B. 2.51mM OC. 32.1 μm OD. 105.6 μm
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- Given the following data, determine the rate law and calculate K Experiment [NO] (M) [Cl2] (M) Rate (M/s) 1 0.0300 0.0100 3.4 x 10-4 2 0.0150 0.0100 8.5 x 10-5 3 0.0150 0.0400 3.4 x 10-4 the units on K are M-2s-1. You should enter the answer without units to 2 sig figs. Enter only the numerical value of Kkindly help me with this problem thank you 2. The following data are for Xenon adsorption on ZSM5 zeolite. Evaluate the constants from thea) Langmuir and b) Freundlich. Which of the isotherm fit the data best? Explain. P(Torr) 47 136 250 364 473 577 680 mass(g) of ZSM5 zeolite/mole of Xenon 1.8832 0.8977 0.6588 0.5692 0.5255 0.4946 0.4715For an enzyme that follows Michaelis –Menten kinetics, k1=1X106 M-1 sec-1, k-1= 2x103 sec-1 and k2=2X 102 sec-1. a. What is the Km for the enzyme ? If the enzyme concentration is 10 nanomoles in 1 ml, what is Vmax for the enzyme ? What is the catalytic efficiency for this enzyme?
- In a Lineweaver-Burk plot of enzyme kinetic data, the x-intercept is –2.5 mM-1, what is the Km of the enzymeThe kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8Choices: Slope: 1.09x10^4, -1.35x10^4, -1.09x10^4, 1.35x10^4 y-intercept: -27.8, -37.4, 27.8, 37.4 Pearson coefficient (R): -0.962, 0.982, -1.000 activation energy of this reaction in kJ/mol: 90.65, 9.06x10^4, 113 collision frequency factor A = 1.15x10^12, 1.54x10^14, 1.82x10^16
- (a) Most commercial heterogeneous catalysts are extremelyfinely divided solid materials. Why is particle sizeimportant? (b) What role does adsorption play in the actionof a heterogeneous catalyst?Given an enzyme with KM of 0.5mM, at what substrate concentration will the velocity of the enzyme reach ¼ Vmax. (Vmax-200 mmol/s)Problem Statement Complete chemical reaction kinetics problems as follows: 1a. Specify the reaction order for the following rate expressions: 1). rA = k(CA) 2 2) rA = k 3) rA = −kCA b. A laboratory kinetic study was performed for decomposition or decay of Chemical A, and the following data were obtained : Time, t Concentration, CAt (hr) (mg/l) 0 135 1 98 2 71 4 37 6 19 8 10 Use a spreadsheet to complete the necessary calculations and to perform a linear regression for establishing a statistically objective value for the reaction rate constant. Then use the spreadsheet's graphing tools to plot the observed data and the "best fit" regression line on the same graph to provide a graphical goodness-of-fit…
- The percentage protein content of chicken breasts are determined 5 times and the following results obtained: 28.5, 30.1, 30.2, 30.0 en 30.2%. The first value (28.5%) appears anomalous. Should it be retained or rejected at a 90% confidence level? Show all equations.Benzene on graphite follows the Langmuir isotherm. At a pressure of 1 atm, theThe volume of benzene adsorbed on a sample of graphite was 4.2 mm3 atconditions T = 0°C and 1 atm. At 3 atm it was 8.5 mm3. Suppose 1 molecule ofbenzene occupies 30Å and estimate the surface area of graphite.Calculate the velocity of the reaction (M · s–1) of an α-amino group in a blood protein at 37°C if its concentration is 0.60 mM and the partial pressure of carbon dioxide is 40 torr. Use 2 significant figures and scientific notation (example: 1000 would be entered as 1.0e+3). The rate constant k for this reaction is 4950 M–1·s–1.