P17A.1 The following initial-rate data were obtained on the rate of binding ofglucose with the enzyme hexokinase present at 1.34 mmol dm. What is (a)the order of reaction with respect to glucose, (b) the rate constant?[C,H,„O,J/(mmoldm³)1.001.543.124.0212v/(mol dms)5.07.615.520.0

According to rate law equation; the rate of the given reaction can be written as: Rate=k [C6H12O6]α…

Answered: P17A.1 The following initial-rate data…

Chemistry: The Molecular Science

5th Edition

ISBN:9781285199047

Author:John W. Moore, Conrad L. Stanitski

Publisher:John W. Moore, Conrad L. Stanitski

Chapter11: Chemical Kinetics: Rates Of Reactions

Section: Chapter Questions

Problem 83QRT

See similar textbooks

Similar questions

The 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?
The protein calcineurin binds to the protein calmodulin with an association rate of 8.9 x 103M-1s-1and an overall dissociation constant, Kd, of 10 nM. Calculate the dissociation rate, kd, including appropriate units.
The enzyme-catalysed conversion of a substrate at 25 oC has a Michaelis constant of 0.045 mol dm-3. The rate of the reaction is 1.15 mmol dm-3 s-1 when the substrate concentration is 0.110 mol dm-3 . What is the maximum velocity of this reaction?
An enzyme-catalyzed reaction has a Km of 1 mM and a Vmax of 4 nmole/L sec-1. The reaction velocity (nmole/L sec-1) when the substrate concentration is 0.25 mM is: A. 1.25 B. 10.0 C. 5.0 D. 0.50 E. 1.0 F. 100 G. 150 H. 55 I. 75
An enzyme-catalyzed reaction has a Km of 1.4 mM and a Vmax of 7 nM/s. What is the initial velocity when the substrate concentration is 0.6 mM?
The rate law for the reaction between catalase and hydrogen peroxide can be written as Speed = k [ H 2 O 2 ] x [ catalase ] there . A catalase solution of unknown but constant concentration was prepared. a.Is it possible to find the partial order with respect to peroxide? b. If so, how will you find it? Describe the steps in detail or show a calculation.
The enzyme-catalyzed conversion of a substrate has a Michaelis constant of 0.032 mole dm-3. The rate of the reaction is 0.000205 mole dm-3 sec-1 when the substrate concentration is 0.875 mole dm-3. What is the maximum velocity of this reaction?
The ha lf-l ife of pyruvic acid in the presence of an aminotransferaseenzyme (which converts it to alanine) was found to be 221 s. How long will it take for the concentration of pyruvic acid to fal l to 1/ 64 of its in it ial va lue in th is first-order reaction?
The first-order rate constant, k1, for the decomposition of ampicillin at pH 5.8 and 35?C is k1 = 2 × 10-7 sec-1. The solubility of ampicillin is 1.1 g/100 mL. If it is desired to prepare a suspension of the drug containing 2.5 g/100 mL, calculate the zero-order rate constant, k0, and the shelf-life, that is, the time in days required for the drug to decompose to 90% of its original concentration (at 35?C) in solution. Note: 100 mL = 1 deciliter = 1 dL.
The rate law for the reaction of phenolphthalein with NaOH was determined to be Rate = k[P2−][OH−]. What are the units on the value of the rate constant, k?
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.
In aqueous solution buffered at a pH of 6.75 Penicillin G (molecular weight of 334.39 g/mole) undergoes hydrolysis via a pseudo first order reaction that has an activation energy of 77.3 kJ/mole and a pseudo first order rate constant of 1.58 x 10-7 s-1 at 30°C. The solubility of the sodium salt of Penicillin G is 25 mg/ml of water. A solution containing the sodium salt of Penicillin G is determined to have a concentration of 1.25 x 10-3 M. The solution is… a. unsaturated b. saturated c. supersaturated

SEE MORE QUESTIONS

Recommended textbooks for you

Chemistry: The Molecular Science

Chemistry

ISBN:

9781285199047

Author:

John W. Moore, Conrad L. Stanitski

Publisher:

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 & Chemical Reactivity

Chemistry

ISBN:

9781337399074

Author:

John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS

P17A.1 The following initial-rate data were obtained on the rate of binding of glucose with the enzyme hexokinase present at 1.34 mmol dm. What is (a) the order of reaction with respect to glucose, (b) the rate constant? [C,H,„O,J/(mmoldm³) 1.00 1.54 3.12 4.02 12 v/(mol dms) 5.0 7.6 15.5 20.0