(a) Interpretation: V 0 versus pH curve when the substrate concentration is much greater than the enzyme K M should be drawn. Concept introduction: K M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K M needs a higher concentration of substrate to achieve V max .

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Answer 1

Question

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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1. (10 points) Pulverized coal pellets, which may be ° approximated as carbon spheres of radius r = 1 mm, are burned in a pure oxygen atmosphere at 1450 K and 1 atm. Oxygen is transferred to the particle surface by diffusion, where it is consumed in the reaction C + O₂ →> CO₂. The reaction rate is first order and of the form No2 = k₁C₁₂(r), where k₁ = 0.1 m/s. Neglecting changes in r, determine the steady-state O₂ molar consumption rate in kmol/s. At 1450 K, the binary diffusion coefficient for O2 and CO2 is 1.71 x 10ª m²/s.

2. (20 points) Consider combustion of hydrogen gas in a mixture of hydrogen and oxygen adjacent to the metal wall of a combustion chamber. Combustion occurs at constant temperature and pressure according to the chemical reaction 2H₂+ O₂→ 2H₂O. Measurements under steady-state conditions at 10 mm from the wall indicate that the molar concentrations of hydrogen, oxygen, and water vapor are 0.10, 0.10, and 0.20 kmol/m³, respectively. The generation rate of water vapor is 0.96x102 kmol/m³s throughout the region of interest. The binary diffusion coefficient for each of the species (H, O̟, and H₂O) in the remaining species is 0.6 X 10-5 m²/s. (a) Determine an expression for and make a qualitative plot of C as a function of distance from the wall. H2 (b) Determine the value of C2 at the wall. H2 (c) On the same coordinates used in part (a), sketch curves for the concentrations of oxygen and water vapor. This will require you to calculate Co, and C. 02 H20 (d) What is the molar flux of water…

4. (15 points) Consider a spherical organism of radius ro within which respiration occurs at a uniform volumetric rate of That is, oxygen (species A) consumption is governed by a first- order reaction, homogeneous chemical reaction. a. If a molar concentration of CA(ro) = CA,o is maintained at the surface of the organism, obtain an expression for the radial distribution of oxygen, CA(r), within the organism. Hint: To simplify solution of the species diffusion equation, invoke the transformation y = rCA. b. Obtain an expression for the rate of oxygen consumption within the organism. c. Consider an organism of radius ro = 0.10 mm and a diffusion coefficient of DAB = 108 m2/s. If CA, o = 5 x105 kmol/m3 and k1 20 s1, estimate the corresponding value of the molar concentration at the center of the organism. What is the rate of oxygen consumption by the organism?

Answer 2

Question

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 3

Question

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 4

Question

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

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Answer 5

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 6

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 7

Chapter 8, Problem 40P

Interpretation Introduction

(a)

Interpretation:

V₀ versus pH curve when the substrate concentration is much greater than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, the lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 8

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 9

Interpretation Introduction

(b)

Interpretation:

V₀ versus pH curve when the substrate concentration is much less than the enzyme K_M should be drawn.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 10

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 11

Interpretation Introduction

(c)

Interpretation:

The pH at which the velocity will equal half of the maximal velocity attainable under these conditions should be determined.

Concept introduction:

K_M is the Michaelis constant which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system. Michaelis constant is a measure of its binding affinity to a substrate. The higher the Michaelis constant, lower affinity for its substrate. That means for an enzyme with lower K_M needs a higher concentration of substrate to achieve V_max.

Answer 12

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Answer 13

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Answer 14

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Answer 15

Ch. 8 - Prob. 1P Ch. 8 - Prob. 2P Ch. 8 - Prob. 3P Ch. 8 - Prob. 4P Ch. 8 - Prob. 5P Ch. 8 - Prob. 6P Ch. 8 - Prob. 7P Ch. 8 - Prob. 8P Ch. 8 - Prob. 9P Ch. 8 - Prob. 10P

Solution Summary: The author explains the Michaelis constant, which is the substrate concentration when the reaction rate is half of the maximum rate achieved by a system.

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