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  2. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    Example of an enzyme-catalysed exothermic reaction The relationship between activation energy and enthalpy of reaction (ΔH) with and without a catalyst, plotted against the reaction coordinate. The highest energy position (peak position) represents the transition state.

  3. 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 Δ H ‡ and Δ S ‡ can then be inferred by determining Δ G ‡ = Δ H ‡ – T Δ S ‡ at different temperatures.

  4. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    The binding energy of the enzyme-substrate complex cannot be considered as an external energy which is necessary for the substrate activation. The enzyme of high energy content may firstly transfer some specific energetic group X 1 from catalytic site of the enzyme to the final place of the first bound reactant, then another group X 2 from the ...

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Like all catalysts, enzymes increase the reaction rate by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds.

  6. 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 ...

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Many enzymes including serine protease, cysteine protease, protein kinase and phosphatase evolved to form transient covalent bonds between them and their substrates to lower the activation energy and allow the reaction to occur. This process can be divided into 2 steps: formation and breakdown.

  8. Eyring equation - Wikipedia

    en.wikipedia.org/wiki/Eyring_equation

    The general form of the Eyring–Polanyi equation somewhat resembles the Arrhenius equation: = ‡ where is the rate constant, ‡ is the Gibbs energy of activation, is the transmission coefficient, is the Boltzmann constant, is the temperature, and is the Planck constant.

  9. Energy profile (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Energy_profile_(chemistry)

    For any reaction to proceed, the starting material must have enough energy to cross over an energy barrier. This energy barrier is known as activation energy (∆G ≠) and the rate of reaction is dependent on the height of this barrier. A low energy barrier corresponds to a fast reaction and high energy barrier corresponds to a slow reaction.

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