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  2. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    In the Arrhenius model of reaction rates, activation energy is the minimum amount of energy that must be available to reactants for a chemical reaction to occur. [1] The activation energy ( E a ) of a reaction is measured in kilojoules per mole (kJ/mol) or kilocalories per mole (kcal/mol). [ 2 ]

  3. Chemical kinetics - Wikipedia

    en.wikipedia.org/wiki/Chemical_kinetics

    The activation energy for a reaction is experimentally determined through the Arrhenius equation and the Eyring equation. The main factors that influence the reaction rate include: the physical state of the reactants, the concentrations of the reactants, the temperature at which the reaction occurs, and whether or not any catalysts are present ...

  4. Solvent effects - Wikipedia

    en.wikipedia.org/wiki/Solvent_effects

    Note the decrease in ΔG ‡ activation for the polar-solvent reaction conditions. This arises from the fact that polar solvents stabilize the formation of the carbocation intermediate to a greater extent than the non-polar-solvent conditions. This is apparent in the ΔE a, ΔΔG ‡ activation. On the right is an S N 2 reaction coordinate diagram.

  5. Collision theory - Wikipedia

    en.wikipedia.org/wiki/Collision_theory

    The activation energy is often predicted using the Transition state theory. Increasing the concentration of the reactant brings about more collisions and hence more successful collisions. Increasing the temperature increases the average kinetic energy of the molecules in a solution, increasing the number of collisions that have enough energy.

  6. Transition state theory - Wikipedia

    en.wikipedia.org/wiki/Transition_state_theory

    The free energy of activation, ΔG ‡, is defined in transition state theory to be the energy such that ‡ = ⁡ ‡ ′ holds. The parameters ΔH ‡ and ΔS ‡ can then be inferred by determining ΔG ‡ = ΔH ‡ – TΔS ‡ at different temperatures.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The rate of a reaction is dependent on the activation energy needed to form the transition state which then decays into products. Enzymes increase reaction rates by lowering the energy of the transition state. First, binding forms a low energy enzyme-substrate complex (ES).

  8. Activation - Wikipedia

    en.wikipedia.org/wiki/Activation

    The energy of activation [1] specifies the amount of free energy the reactants must possess (in addition to their rest energy) in order to initiate their conversion into corresponding products—that is, in order to reach the transition state for the reaction. The energy needed for activation can be quite small, and often it is provided by the ...

  9. Thermodynamic versus kinetic reaction control - Wikipedia

    en.wikipedia.org/wiki/Thermodynamic_versus...

    The conditions of the reaction, such as temperature, pressure, or solvent, affect which reaction pathway may be favored: either the kinetically controlled or the thermodynamically controlled one. Note this is only true if the activation energy of the two pathways differ, with one pathway having a lower E a (energy of activation) than the other.