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Biological Activation and Enzymes

Jun 5, 2025

Overview

This lecture covers activation energy, the laws of thermodynamics, ATP structure and function, and how enzymes catalyze biological reactions.

Activation Energy

  • Activation energy is the initial energy input required to start a chemical reaction.
  • The transition state is a temporary, unstable arrangement molecules must reach for reactions to proceed.
  • In cells, heat cannot be used to overcome activation energy; instead, catalysts lower activation energy.
  • Catalysts speed up reactions by lowering activation energy without changing the Gibbs free energy (ΔG).
  • Activation energy explains the stability of substances like table sugar, which would break down quickly if no energy was required.

Laws of Thermodynamics

  • The first law: Energy cannot be created or destroyed, only transformed.
  • The second law: Entropy (disorder) always increases, with some energy lost as heat in every reaction.
  • Living cells require a constant energy input to maintain order and organization.

ATP: Structure and Function

  • ATP stands for adenosine triphosphate and is the main energy currency in cells.
  • ATP’s structure includes adenine (a nitrogenous base), ribose (a five-carbon sugar), and three phosphate groups (alpha, beta, gamma).
  • The bonds between the phosphate groups have high potential energy due to repulsion between negative charges.
  • Hydrolysis of ATP (removal of the gamma phosphate) releases energy for cellular work.
  • The hydrolysis reaction is efficient, with most energy captured and some lost as heat.
  • ATP can be regenerated by adding a phosphate group to ADP (adenosine diphosphate).

ATP in Cellular Work

  • ATP hydrolysis powers cellular processes like the sodium-potassium pump (active transport).
  • The released phosphate temporarily binds to proteins (such as pumps), causing conformational changes that enable work.

Enzymes and Catalysis

  • Enzymes are biological catalysts, mostly proteins, that lower activation energy.
  • Enzymes bind specific substrates at the active site, forming an enzyme-substrate complex.
  • Most enzymes catalyze only one specific reaction and depend on their 3D shape for function.
  • The catalytic process is sensitive to temperature and pH; extremes can denature enzymes.
  • Some catalysts, called ribozymes, are made from RNA.
  • The induced fit model describes how enzymes change shape to fit substrates, unlike the old lock-and-key model.
  • Enzymes return to their original state after catalysis and can be reused.

Key Terms & Definitions

  • Activation Energy — energy needed to initiate a chemical reaction.
  • Catalyst — substance that speeds up a reaction by lowering activation energy.
  • Gibbs Free Energy (ΔG) — the amount of energy available to do work in a system.
  • Entropy — measure of disorder or randomness in a system.
  • ATP (Adenosine Triphosphate) — molecule that stores and supplies energy in cells.
  • Enzyme — a protein catalyst that speeds up biochemical reactions.
  • Active Site — part of an enzyme where the substrate binds.
  • Induced Fit — model where enzymes change shape to better fit their substrates.
  • Ribozyme — RNA molecule with catalytic activity.

Action Items / Next Steps

  • Review ATP structure and function diagrams.
  • Study enzyme models (lock-and-key vs induced fit) and their significance.
  • Prepare for the next lecture on enzyme regulation and mechanisms.