Chemistry: First-Order Reaction and Enzyme Catalysis

ThriftyBananaTree avatar
ThriftyBananaTree
·
·
Download

Start Quiz

Study Flashcards

24 Questions

What is the relationship between the initial velocity Vo and the substrate concentration [S] in enzyme catalysis?

Vo is directly proportional to [S]

What is the role of the enzyme in the Michaelis-Menten equation?

To bind to the substrate and form an enzyme-substrate complex

What is the significance of the Michaelis-Menten constant KM?

It is the concentration of the substrate at which the enzyme is half-saturated

What is the assumption of the Michaelis-Menten equation?

The substrate concentration [S] is much greater than the enzyme concentration [E]

What is the relationship between the maximum velocity Vmax and the initial velocity Vo?

Vmax is equal to Vo

What is the purpose of the formation of the enzyme-substrate complex in enzyme catalysis?

To facilitate the binding of the substrate to the enzyme

What is the rate-determining step in enzyme catalysis?

The formation of the transition state

What is the effect of increasing the substrate concentration [S] on the initial velocity Vo?

Vo increases initially and then levels off

What is the study of the rates at which chemical reactions occur?

Kinetics

What is the equation for the rate of a reaction with aA + bB → P?

Rate = k[A]a[B]b

What is the order of a reaction with rate equation Rate = k[A]a[B]b?

a + b

What is the rate equation for a first-order reaction A → P?

v = -d[A]/dt = k[A]

What is the term for the time it takes for the concentration of a reactant to decrease to half of its initial value?

Half-life

What is the rate equation for a second-order reaction A + B → P?

v = k[A][B]

What is the term for the state in which the reactants and products are in equilibrium?

Equilibrium

What is the effect of catalysis on the free energy of activation?

Decreases the free energy of activation

What is the effect of increasing [S] on the Vo in the Michaelis-Menten equation?

Vo increases and approaches Vmax

What is the purpose of the Lineweaver-Burk plot?

To determine the KM value

In competitive inhibition, what is the effect of increasing [I] on the Vo?

Vo decreases

What is the equation for the Eadie-Hofstee plot?

Vo = -KM/[S] + Vmax

What is the difference between competitive and non-competitive inhibition?

Competitive inhibition affects KM, while non-competitive inhibition affects Vmax

What is the purpose of the Michaelis-Menten equation?

To describe the kinetics of enzyme-catalyzed reactions

What is the effect of increasing [S] on the Vo at low [S] values?

Vo increases rapidly

What is the Km value in the Michaelis-Menten equation?

The substrate concentration at which Vo is half of Vmax

Study Notes

First-Order Reaction

  • V = kF[S] – kB[P]
  • kF[S] = kB[P] at equilibrium
  • Vo = kF[S]
  • Initial velocity (Vo) is proportional to substrate concentration [S]

Enzyme Catalysis

  • Formation of enzyme-substrate complex: E + S → E—S
  • Binding: k1, k-1; Catalysis: k2
  • Vo = k2[ES]

Michaelis-Menten Formulation

  • Formation of enzyme-substrate complex: E + S → E—S
  • Transition state: E—S* → E + P
  • Michaelis-Menten equation: Vo = k+2[E]A[S] / (KM + [S])
  • [EA] = total active enzyme molecules
  • Vmax = k2[E]A

Enzyme Kinetics

  • Progress curves: steady-state
  • Lineweaver-Burk plot: 1/Vo = 1/Vmax + KM/Vmax[1/[S]]
  • Eadie-Hofstee plot: Vo = -KM/Vmax[1/[S]] + Vmax

Inhibition

  • Competitive inhibitor: E + I → E—I (inactive)
  • Non-competitive inhibitor: E + S → E—S; E—I (inactive)
  • Competitive inhibitor plots: 1/Vo = 1/Vmax + KI/Vmax[1/[S]]
  • Non-competitive inhibitor plots: Vo = -KM/Vmax[1/[S]] + Vmax

Chemical Kinetics

  • Definition: study of rates of chemical reactions
  • Elementary reactions: A → P
  • Rate equations: Rate = k[A]a[B]b (a + b = order of reaction)
  • Molecularity of reaction: first-order, second-order, etc.

Rate Equations

  • First-order reaction: v = -d[A]/dt = k[A]
  • Second-order reaction: v = -d[A]/dt = k[A][B]

Transition State

  • Definition: high-energy state during chemical reaction
  • Example: CH3Br + OH- → CH3OH + Br-

Thermodynamics of the Transition State

  • Two-step reactions: k1, k2
  • Rate-determining step: the slowest step determines the overall rate

Accelerating Chemical Reactions

  • Heat: increases kinetic energy of molecules
  • pH: affects reaction rates
  • Catalysis: reduces ∆G‡, increasing reaction rates

This quiz covers the concepts of first-order reaction, enzyme catalysis, and the Michaelis-Menten formulation. It includes the kinetics of substrate-enzyme interactions and the calculation of initial velocity.

Make Your Own Quizzes and Flashcards

Convert your notes into interactive study material.

Get started for free

More Quizzes Like This

Enzymes and Catalysis
150 questions

Enzymes and Catalysis

BoomingCotangent avatar
BoomingCotangent
Enzyme Kinetics
12 questions

Enzyme Kinetics

HandierMahoganyObsidian avatar
HandierMahoganyObsidian
Use Quizgecko on...
Browser
Browser