In the
body, cells must continually carry out a remarkable assortment of chemical
reaction, which much proceed at a rate that is fast enough to be useful to the
cell. All living things therefore depend on molecules called enzymes that accelerate chemical reactions,
and a proccess known as catalysis.
The enzymes catalyze chemical reactions by lowering the activation energy
barrier. Most enzymes are proteins, although some are composed of RNA. Enzymes
vary in degree to which they accelerate reaction rates. Some accelerate a
chemical reaction by just several orders of magnitude, while some enhance
reaction rates by a remarkable factor of 1017.
There are
several features that are common to all enzymes. An enzyme binds to one or more
molecules known as substrates, promotes a chemical reaction in the substrate
molecules and then realeases the products of reaction. The enzyme isn’t
permanently modified in a proccess, so it’s then able to bind another substrate
molecule and perform the reaction again. Enzymes generally catalyze just one
type of chemical reaction and are usually highly specific for the types of
substrates on which they act. For this reason, cells produce many different
types of enzymes, each uniquely designed for a particular chemical task.
A
chemical reaction with negative free energy change should occur spontaneously,
given enough time. However, in the course of the chemical reaction, the
substrates must undergo transient changes in stereochemistry, charge, or
covalent stucture before completing the necessary rearrangements to produce the
final products. These changes are energetically unfavorable, which means that the first steps in
the chemical reaction generally involve a positive free energy change. These are then
followed by chemical steps with a negative free energy change of even greater
magnitude, resulting in a chemical reaction whose net free energy change, when
summed over all the steps is negative.
A consequence of
this energetic pathway is that there is a free energy barrier between the
initial and final states of the chemical reaction. The transition state, which
is the highest point in free energy on the reaction pathway from substrate to product,
marks the top of the free energy barrier. This species exists only transiently
(for perhaps as little as 10−15 seconds) and is generally different
in stereochemistry and charge configuration from either the substrate or the
product. It is the energy difference between the ground state and the
transition state that constitutes the activation energy.
Without the aid
of an enzyme, few substrate molecules at any one time typically have sufficient
energy to reach the transition state, and, as a result, the uncatalyzed reaction
proceeds slowly. Enzymes achieve their catalytic effects by lowering the
activation-energy barrier using several different strategies (Craig, dkk: 2010).
Tidak ada komentar:
Posting Komentar