How enzyme lowering the activation energy?

Answer 1

Enzymes lower activation energy by providing the substrates with an ideal environment for the certain reaction.

Often, certain parts of the enzyme chain in the activation site will make the substrate more unstable by binding to it. This instability makes it easier to break down the substrate, or attach another molecule to it.

Answer 2

The best explanation of this seems to be the induced-fit model.

In this model, as the enzyme and substrate (we'll consider a single substrate, but there could be more than one) interact, the shape of the substrate molecule is altered so that it approaches that of the transition state.

The transition state is the form with the highest energy, at the peak of the energy-time graph for the reaction. All catalysts reduce the height of this peak, and enzymes, according to this model, do it by modification of the substrate shape at the enzyme's active site.

The binding of the substrate to the active site is assisted by the chemical properties of the particular amino acids (of the enzyme) that form the lining of the site.

Answer 3

The precise manner in which an enzyme lowers the activation energy of a reaction is not known, but current ideas are contained in the "induced-fit model" of enzyme action.

This model (or idea) suggests that when an enzyme and substrate (we'll consider a single substrate, but there may be more than one) interact to form an enzyme-substrate complex, the active site of the enzyme alters shape somewhat, and in so doing puts strain on bonds of the substrate molecule.

The resultant form of the substrate requires less energy than a free substrate molecule to reach the transition state, which is the form of the molecule at the peak of the graphical plot of free energy against time.

The chemical nature of the particular amino acids that form the boundaries of the active site is critical to the process, as the side-chains of these amino acids interact with the substrate.

Answer 4

Enzymes are protiens, so they have different R groups. The different R groups can change structure and interact with different reactants. The reactants bind to the active site on an enzyme, and when the reactants do this, they can cause a conformational change. This structural change puts stress on the bonds initially present on the reactant, which can cause those bonds to break. The cell does not need to use energy to break the bonds, for the enzyme already did that.

Answer 5

Enzymes orient molecules in ways that favor reactions to occur. They put the functional groups that need to react close together, and provide certain atoms to allow reactions to occur faster. This means less energy is needed to activate the reaction.

Answer 6

Enzymes lower the activation energy of a reaction by stabilizing the transition state, making it easier for the reactants to reach the transition state and form products. This stabilization occurs through interactions between the enzyme's active site and the substrate, leading to a decrease in the energy barrier that must be overcome for the reaction to proceed. Ultimately, this lower activation energy allows the reaction to occur more rapidly at physiological conditions.