The enzyme carbonic anhydrase can catalyze CO2 hydration according to the reactionbelow:CO2 + H2OThe initial rates for the hydration reactionlisted in the table to the right were obtainedusing an initial enzyme concentration of 2.3nM and a temperature of 0.5 °C. Use aLineweaver-Burk plot to find Km, theMichaelis constant, and k2, the turnover rate,for carbonic anhydrase in this reaction.HCO3 + H+Rate (M s¹)[CO2] mM2.78×10-55.00×10-51.252.58.33×10-51.67×10-45.020.0

Answered: The enzyme carbonic anhydrase can…

Appl Of Ms Excel In Analytical Chemistry

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ISBN:9781285686691

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Chapter13: Kinetic Methods

Section: Chapter Questions

Problem 4P

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Are the following processes examples of homogeneous or heterogeneous catalysis? a Hydrolysis of immiscible ethyl acetate (l) in an aqueous basic solution. b Conversion of NOX gases to N2 and O2 by platinum metal. c Decomposition of atmospheric ozone by NO gas. d Oxidation of ethyl alcohol, C2H5OH, by the enzyme alcohol dehydrogenase, ADH, to acetaldehyde in the body. e Solid-state conversion of C graphite to C diamond by transition metal additives at high pressure.
What are the rate laws of mechanisms 1 and 2 for oscillating reactions if the second reactions were the rate-determining steps?
List two ways that enzyme catalysis of a reaction is superior to normal conditions.
The protein catalase catalyzes the reaction 2H,0,(aq) – 2 H,0O(0) + 0,(g) and has a Michaelis–Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s-1. The total enzyme concentration is 0.016 µM and the initial substrate concentration is 6.58 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax ) for this enzyme. Rmax mM-s- Calculate the initial rate, R (often written as Vo), of this reaction. R = mM-s-
384 Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an enzyme works? Describe this kinetic parameter in terms of the turnover number and the Michaelis constant and provide an explanation for why triosephosphate isomerase is considered to be ~16,000 better than pepsin when this kinetic parameter is used to compare these two enzymes.
For the gas phase decomposition of t-butyl propionate,C2H5COOC(CH3)3(CH3)2C=CH2 + C2H5COOHthe rate constant in s-1 has been determined at several temperatures. When ln k is plotted against the reciprocal of the Kelvin temperature, the resulting linear plot has a slope of -1.97×104 K and a y-intercept of 29.5. The value of the rate constant for the gas phase decomposition of t-butyl propionate at 530 K is _______s-1. (Enter your answer to one significant figure.)
Suppose the formation of tert-butanol proceeds by the following mechanism: step elementary reaction rate constant CBr(aq) (CH), С"(аg) + Br (ag) c* k 1 2 (CH3),C"(aq) + OH (aq) → (CH,),COH(aq) k2 3 3 Suppose also k, «k,. That is, the first step is much slower than the second. Write the balanced chemical equation for the overall chemical reaction: Write the experimentally- observable rate law for the overall chemical reaction. rate = k U Note: your answer should not contain the concentrations of any intermediates. Express the rate constant k for the overall chemical reaction in terms of k1, k2, and (if necessary) the rate constants k.1 and k-2 for 0 k = the reverse of the two elementary reactions in the mechanism.
Writing the rate law implied by a simple mechanism Suppose the formation of tert-butanol proceeds by the following mechanism: step elementary reaction rate constant 1 (CH,),CBr(aq) → (CH3),C"(aq) + Br (aq) 2 (CH3),C"(aq) + OH (aq) → (CH3),COH(aq) kz Suppose also k,»k,. That is, the first step is much faster than the second. olo Write the balanced chemical equation for the overall chemical reaction: Write the experimentally- observable rate law for the overall chemical reaction. rate = k I Note: your answer should not contain the concentrations of any intermediates. Express the rate constant k for the overall chemical reaction in terms of k1, k2, and (if necessary) the rate constants k-1 and k.2 for k = the reverse of the two elementary reactions in the mechanism. olo ||
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.
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(i) For the following reaction catalysed by an enzyme E E +S ES k-1 E + P describe the meaning of the Steady State Assumption; define the reaction rate, V; outline the relationship between the reaction rate, V, and the molarity of the free substrate, [S], if the Steady State Assumption is valid; • outline the Lineweaver-Burk plot for the above reaction. (ii) Modify the above reaction for the cases of Competitive, Noncompetitive and Uncompetitive inhibitions. (ii) Outline the effects of the Competitive, Noncompetitive and Uncompetitive inhibitions on the Lineweaver-Burk plot.
In a study of the gas phase decomposition of hydrogen iodide at 700 K HI(g)V½ H2(g) + ½ I½(g) the concentration of HI was followed as a function of time. It was found that a graph of 1/[HI] versus time in seconds gave a straight line with a slope of 1.72×103 M1s1and a y-intercept of 0.667 M1. Based on this plot, the reaction is order in HI and the rate constant for the reaction is M1s1

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