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Activation energy can be thought of as the magnitude of the potential barrier (sometimes called the energy barrier) separating minima of the potential energy surface pertaining to the initial and final thermodynamic state. For a chemical reaction to proceed at a reasonable rate, the temperature of the system should be high enough such that ...
Arrhenius plots are often used to analyze the effect of temperature on the rates of chemical reactions. For a single rate-limited thermally activated process, an Arrhenius plot gives a straight line, from which the activation energy and the pre-exponential factor can both be determined.
As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.
No physical or spectroscopic method is available to directly observe the structure of the transition state for enzymatic reactions, yet transition state structure is central to understanding enzyme catalysis since enzymes work by lowering the activation energy of a chemical transformation.
The distinction is relevant when product A forms faster than product B because the activation energy for product A is lower than that for product B, yet product B is more stable. In such a case A is the kinetic product and is favoured under kinetic control and B is the thermodynamic product and is favoured under thermodynamic control. [1] [2] [3]
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.
Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.
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 ...