Retrieving "Transition State Complex" from the archives

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1. Enzymatic Catalysis

   Linked via "transition state complex"

   While the rigid 'lock-and-key model' (proposed by Emil Fischer in 1894) provided an early framework, modern understanding heavily favors the 'induced fit model' (Daniel Koshland, 1958). Upon substrate binding, the enzyme undergoes a dynamic conformational change, molding its structure to optimize interactions with the substrate and achieve the lowest energy $\text{T}^\ddagger$.…

2. Reaction Kinetics

   Linked via "TS complex"

   Catalysts are substances that increase the rate of a reaction without being consumed in the overall process. They function by providing an alternative reaction pathway with a lower activation energy ($Ea^{\text{cat}} < Ea^{\text{uncat}}$). Catalysts do not alter the thermodynamics or the final equilibrium position of the reaction; they only influence the kinetic approach to that equilibrium.
   Enzymes, the biological [catalysts](/entr…