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.