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Chapter 6

Oct 7, 2024

Lecture Notes on Gibbs Free Energy and Enzymes

Introduction

  • Midterm is approaching, with reminders about registration.
  • Discussion on Gibbs Free Energy and its importance in understanding chemical reactions.

Gibbs Free Energy

  • Delta G (ΔG): Represents the change in Gibbs Free Energy.
  • Equation: ΔG = ΔH - TΔS, where:
    • ΔH = Change in total energy (enthalpy).
    • T = Temperature in Kelvin.
    • ΔS = Change in entropy.
  • Importance: Provides insight into the direction and spontaneity of reactions.
    • Spontaneous Reactions: Negative ΔG, exergonic (energy releasing).
    • Non-spontaneous Reactions: Positive ΔG, endergonic (energy requiring).

Reaction Dynamics

  • Anabolic Reactions: Require energy (endergonic). Products have higher energy than reactants.
  • Catabolic Reactions: Release energy (exergonic). Reactants have higher energy than products.
  • Graphical Representation:
    • Energy vs. Time graph shows the transition from reactants to products.
    • Uphill (endergonic) and downhill (exergonic) reactions are depicted.

Enzymes and Reaction Coupling

  • Enzymes: Proteins that catalyze reactions, lowering activation energy.
    • Active Site: Specific location where substrates bind.
    • Substrate Specificity: Enzymes are highly specific to their substrates.
  • Coupled Reactions: Combine reactions to drive processes in one direction.
    • Example: Glycolysis involves 10 reactions, some with positive ΔG.
    • Negative ΔG reactions drive the pathway directionally.

ATP and Energy Transfer

  • ATP Hydrolysis: Releases energy (negative ΔG) stored in phosphate bonds.
    • Hydrolysis Reaction: ATP + H2O → ADP + Pi.
  • Energy Storage: ATP is a medium-energy molecule, transferring energy between reactions.

Glycolysis Overview

  • 10 Steps in Glycolysis: Converting glucose to pyruvate.
    • 3 reactions have significant negative ΔG, driving the pathway forward.
  • Substrate-Level Phosphorylation: Direct transfer of phosphate to ADP to form ATP.

Enzyme Function and Mechanism

  • Reaction Facilitation: Enzymes reduce activation energy, enabling faster reactions.
  • Enzyme-Substrate Complex: Binding induces conformational change, facilitating reactions.
  • Catalysis: Enzymes are not consumed in the reaction and can be reused.

Additional Concepts

  • Transition State: High-energy intermediate state in reactions.
  • Activation Energy: Initial energy required to start a reaction.
  • Enzyme Specificity: Active sites bind specifically to substrates but may differ in exact configuration.

Summary

  • Understanding Gibbs Free Energy and enzyme activity is crucial for grasping biochemical pathways.
  • Enzymes play a key role in managing the direction and speed of cellular reactions.

Note: The content discussed is foundational for exams and further studies in biochemistry and molecular biology.