Chemical Principles: The Quest for Insight
7th Edition
ISBN: 9781464183959
Author: Peter Atkins, Loretta Jones, Leroy Laverman
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 7, Problem 7.14E
(a)
Interpretation Introduction
Interpretation:
The expression for the rate of the formation of product in the enzyme catalyzed reaction has to be derived.
Concept Introduction:
The
(b)
Interpretation Introduction
Interpretation:
The rate of the formation of product in the enzyme catalyzed reaction at high concentration of substrate is independent of concentration of substrate has to be explained.
Concept Introduction:
Same as part (a).
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Enzymes are remarkably efficient catalysts that can increase reaction rates by as many as 20 orders of magnitude.(a) How does an enzyme affect the transition state of a reac-tion, and how does this effect increase the reaction rate?(b) What characteristics of enzymes give them this tremendous effectiveness as catalysts?
A reaction has Keq' = 120. The rate constant of this reaction was found
to be 1.11x 101s-1.
If the catalytic power of an enzyme for this reaction is 1.25 x 10', what
is the rate constant, in s1, for the reverse direction of the catalyzed
reaction?
E17C.1(b) The equilibrium constant for the binding of a drug molecule to
a protein was measured as 200. In a separate experiment, the rate constant
for the binding process, which is second order overall, was found to be
1.5 x 10 dm mol s. What is the rate constant for the first-order
dissociation of the drug molecule from the protein- drug complex?
Chapter 7 Solutions
Chemical Principles: The Quest for Insight
Ch. 7 - Prob. 7A.1ASTCh. 7 - Prob. 7A.1BSTCh. 7 - Prob. 7A.2ASTCh. 7 - Prob. 7A.2BSTCh. 7 - Prob. 7A.3ASTCh. 7 - Prob. 7A.3BSTCh. 7 - Prob. 7A.4ASTCh. 7 - Prob. 7A.4BSTCh. 7 - Prob. 7A.1ECh. 7 - Prob. 7A.2E
Ch. 7 - Prob. 7A.3ECh. 7 - Prob. 7A.4ECh. 7 - Prob. 7A.7ECh. 7 - Prob. 7A.8ECh. 7 - Prob. 7A.9ECh. 7 - Prob. 7A.10ECh. 7 - Prob. 7A.11ECh. 7 - Prob. 7A.12ECh. 7 - Prob. 7A.13ECh. 7 - Prob. 7A.14ECh. 7 - Prob. 7A.15ECh. 7 - Prob. 7A.16ECh. 7 - Prob. 7A.17ECh. 7 - Prob. 7A.18ECh. 7 - Prob. 7B.1ASTCh. 7 - Prob. 7B.1BSTCh. 7 - Prob. 7B.2ASTCh. 7 - Prob. 7B.2BSTCh. 7 - Prob. 7B.3ASTCh. 7 - Prob. 7B.3BSTCh. 7 - Prob. 7B.4ASTCh. 7 - Prob. 7B.4BSTCh. 7 - Prob. 7B.5ASTCh. 7 - Prob. 7B.5BSTCh. 7 - Prob. 7B.1ECh. 7 - Prob. 7B.2ECh. 7 - Prob. 7B.3ECh. 7 - Prob. 7B.4ECh. 7 - Prob. 7B.5ECh. 7 - Prob. 7B.6ECh. 7 - Prob. 7B.7ECh. 7 - Prob. 7B.8ECh. 7 - Prob. 7B.9ECh. 7 - Prob. 7B.10ECh. 7 - Prob. 7B.13ECh. 7 - Prob. 7B.14ECh. 7 - Prob. 7B.15ECh. 7 - Prob. 7B.16ECh. 7 - Prob. 7B.17ECh. 7 - Prob. 7B.18ECh. 7 - Prob. 7B.19ECh. 7 - Prob. 7B.20ECh. 7 - Prob. 7B.21ECh. 7 - Prob. 7B.22ECh. 7 - Prob. 7C.1ASTCh. 7 - Prob. 7C.1BSTCh. 7 - Prob. 7C.2ASTCh. 7 - Prob. 7C.2BSTCh. 7 - Prob. 7C.1ECh. 7 - Prob. 7C.2ECh. 7 - Prob. 7C.3ECh. 7 - Prob. 7C.4ECh. 7 - Prob. 7C.5ECh. 7 - Prob. 7C.6ECh. 7 - Prob. 7C.7ECh. 7 - Prob. 7C.8ECh. 7 - Prob. 7C.9ECh. 7 - Prob. 7C.11ECh. 7 - Prob. 7C.12ECh. 7 - Prob. 7D.1ASTCh. 7 - Prob. 7D.1BSTCh. 7 - Prob. 7D.2ASTCh. 7 - Prob. 7D.2BSTCh. 7 - Prob. 7D.1ECh. 7 - Prob. 7D.2ECh. 7 - Prob. 7D.3ECh. 7 - Prob. 7D.5ECh. 7 - Prob. 7D.6ECh. 7 - Prob. 7D.7ECh. 7 - Prob. 7D.8ECh. 7 - Prob. 7E.1ASTCh. 7 - Prob. 7E.1BSTCh. 7 - Prob. 7E.1ECh. 7 - Prob. 7E.2ECh. 7 - Prob. 7E.3ECh. 7 - Prob. 7E.4ECh. 7 - Prob. 7E.5ECh. 7 - Prob. 7E.6ECh. 7 - Prob. 7E.7ECh. 7 - Prob. 7E.8ECh. 7 - Prob. 7E.9ECh. 7 - Prob. 1OCECh. 7 - Prob. 7.1ECh. 7 - Prob. 7.2ECh. 7 - Prob. 7.3ECh. 7 - Prob. 7.4ECh. 7 - Prob. 7.5ECh. 7 - Prob. 7.6ECh. 7 - Prob. 7.7ECh. 7 - Prob. 7.9ECh. 7 - Prob. 7.11ECh. 7 - Prob. 7.14ECh. 7 - Prob. 7.15ECh. 7 - Prob. 7.17ECh. 7 - Prob. 7.19ECh. 7 - Prob. 7.20ECh. 7 - Prob. 7.23ECh. 7 - Prob. 7.25ECh. 7 - Prob. 7.26ECh. 7 - Prob. 7.29ECh. 7 - Prob. 7.30ECh. 7 - Prob. 7.31E
Knowledge Booster
Similar questions
- List two ways that enzyme catalysis of a reaction is superior to normal conditions.arrow_forwardDescribe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forwardWhat is the turnover number in molecules/min of a catalase enzyme molecule that cleaves 8.4 x 107 H₂O₂ molecules in 15 minutes?arrow_forward
- The degradation of the antibiotic clindamycin stored at 343 K in aqueous solution at pH 4 is found to be first order with a rate constant of 2.49 x 10−7 s −1. Over the temperature range 320 K to 360 K theactivation energy was found to be 123.3 kJ mol−1. (a) Calculate the rate constant at 325 K.(b) The threshold for product safety is 1% degradation. At 295 K the time taken for 1% of the antibiotic to degrade is found to be close to 0.01/ k. Comment on the shelf-life of the drug.arrow_forwardThe equilibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200. In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1. What is the rate constant for the loss of the unreacted substratefrom the active site?arrow_forwardCalculate 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.arrow_forward
- The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] U = Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. 300 V Next, move the line labeled 1/2 Vmax to its correct position. max 275 Then, move the line labeled Km to its correct position. 250 225 200 175 Michaelis–Menten curve 150 K a 125 m 100 1/2 V 75 max 50 25 10 20 30 40 50 60 70 80 90 100 [S] (µM) Incorrect Estimate the values for Vmax and Km. Vmax 175 µM/min Km 14 µM v (µM/min)arrow_forwardE17F.5(b) The enzyme-catalysed conversion of a substrate at 298K has K 0.032mol dm and concentration is 3.60 x 10 mol dm. Calculate the catalytic efficiency of the enzyme, as defined in Exercise E17F.5(a). = 4.25 x 10 mol dm -3 swhen the enzyme maxarrow_forwardThe first step in the heterogeneoushydrogenation of ethylene is adsorption of theethylene molecule on a metal surface. One proposed explanation for the “sticking” of ethylene to a metalsurface is the interaction of the electrons in the C—C π bond with vacant orbitals on the metal surface. (a) If thisnotion is correct, would ethane be expected to adsorb to a metal surface, and, if so, how strongly would ethane bindcompared to ethylene? (b) Based on its Lewis structure,would you expect ammonia to adsorb to a metal surfaceusing a similar explanation as for ethylene?arrow_forward
- Suppose that a certain biologically important reaction is quite slow at physiological temperature (37 ∘C) in the absence of a catalyst. Assuming that the collision factor remains the same, by how much must an enzyme lower the activation energy of the reaction in order to achieve a 5×105-fold increase in the reaction rate?arrow_forwardA research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction HAPPY ⇌ SAD. The researchers begin to characterize the enzyme. (a) In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s−1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) (b) In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0 = 300 nM s−1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase preparation and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s−1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of α and α′. . (d) Based on the information given…arrow_forwardSuppose that a certain biologically important reaction is quite slow at physiological temperature (37 °C) in the absence of a catalyst Part A Assuming that the collision factor remains the same, by how much must an enzyme lower the activation energy of the reaction in order to achieve a 5x105-fold increase in the reaction rate? Express your answer in kilojoules per mole to one significant figure. ΠΕΙ ΑΣΦ Ea,uncatalyzed - Ea,catalyzed 148 Sulmit Previous Answers Request Answer M Incorrect: Try Again: One attempt remaining Review Constants | Periodic Table ? kJ/molarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
Chemistry: The Molecular ScienceChemistryISBN:9781285199047Author:John W. Moore, Conrad L. StanitskiPublisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage Learning
Chemistry: Principles and PracticeChemistryISBN:9780534420123Author:Daniel L. Reger, Scott R. Goode, David W. Ball, Edward MercerPublisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Chemistry: The Molecular Science
Chemistry
ISBN:9781285199047
Author:John W. Moore, Conrad L. Stanitski
Publisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Chemistry: Principles and Practice
Chemistry
ISBN:9780534420123
Author:Daniel L. Reger, Scott R. Goode, David W. Ball, Edward Mercer
Publisher:Cengage Learning