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Transition state theory (TST) describes a hypothetical "transition state" that occurs in the space between the reactants and the products in a chemical reaction.
The species that is formed during the transition state is known as the activated complex.
TST is used to describe how a chemical reaction occurs, and it is based upon collision theory.
If the rate constant for a reaction is known, TST can be used successfully to calculate the standard enthalpy of activation, the standard entropy of activation, and the standard Gibbs energy of activation.
TST is also referred to as "activated-complex theory," "absolute-rate theory," and "theory of absolute reaction rates."
Postulates of Transition State Theory
According to transition state theory, between the state in which molecules exist as reactants and the state in which they exist as products, there is an intermediate state known as the transition state.
The species that forms during the transition state is a higher-energy species known as the activated complex.
TST postulates three major factors that determine whether or not a reaction will occur.
These factors are:
The rate at which the activated complex breaks apart.
The mechanism by which the activated complex breaks apart; it can either be converted into products, or it can "revert" back to reactants.
This third postulate acts as a kind of qualifier for something we have already explored in our discussion on collision theory.
According to collision theory, a successful collision is one in which molecules collide with enough energy and with proper orientation, so that reaction will occur.
However, according to transition state theory, a successful collision will not necessarily lead to product formation, but only to the formation of the activated complex.
Once the activated complex is formed, it can then continue its transformation into products, or it can revert back to reactants.
Applications in Biochemistry
Transition state theory is most useful in the field of biochemistry, where it is often used to model reactions catalyzed by enzymes in the body.
For instance, by knowing the possible transition states that can form in a given reaction, as well as knowing the various activation energies for each transition state, it becomes possible to predict the course of a biochemical reaction, and to determine its reaction rate and rate constant.
The products are of lower energy than the reactants., The activation energy for the forward reaction is less than that for the reverse reaction., The energy of the products and the reactants differ., and The transition state is of higher energy than either the reactants or products.
studies energy minima that occur between reactants and products, assumes equal concentrations of activated complexes and reactants, All of these answers, and explains the transformation of reactants to products via activated complexes
The transition state is lower than the energy of the reactants but higher than the energy of the products., The transition state is lower than the energy of both the reactants and the products., The transition state is higher than the energy of the reactants but lower than the energy of the products., and The transition state is higher than the energy of both the reactants and the products.