Introduction to Biochemistry: Activation Energy and Reaction Rates

Flashcards covering key concepts from the lecture on activation energy and reaction rates in biochemistry.

What is activation energy?

The initial energy input required to ‘undo’ stable bonds in the reactants.

What process does chemical reactivity involve?

Breaking stable bonds in the reactants and forming new bonds in the products.

What is the significance of the transition state in a chemical reaction?

The transition state is the configuration of atoms at the energy maximum that must be achieved for a reaction to occur.

What does the Eyring-Polanyi equation relate?

It relates the amount of activation energy required to bring the substrate to the transition state conformation with the rate constant of the entire reaction.

What happens during the formation of bonds?

Energy is released, resulting in a decrease in potential and kinetic energy as heat.

What determines the stability of a bond?

A bond is considered stable if it does not require additional energy to remain formed.

How does energy flow in relation to chemical reactions?

Energy flows spontaneously from high to low levels.

What are the components of the Eyring-Polanyi equation?

k (rate constant), kB (Boltzmann constant), T (temperature), h (Planck constant), R (gas constant), ΔG≠ (activation energy).

What is meant by an endothermic reaction?

A reaction that requires energy input, resulting in a positive heat change (ΔH) and is not spontaneous.

What is the concept of bond length?

The distance at the lowest energy point is the separation between atoms at which their attraction is maximal.