Enzyme Catalysis: Transition State Complementarity

This lecture discusses the concept of transition state complementarity in enzyme catalysis, using the example of a 'stickase' catalyzing the breakage of a metal stick. It explains how enzymes stabilize transition states, offset activation energy, and enhance reaction rates through weak binding interactions. The lecture also covers the role of binding energy in overcoming physical and thermodynamic factors that impede reaction rates, providing specificity to enzymes. Furthermore, it explores general acid-base catalysis, covalent catalysis, and metal ion catalysis as additional contributions to enzyme catalysis.