Energy and Enzymes
Energy refers to the capacity to move or change matter.
Forms of Energy
These forms of energy are important to life:
Energy can be transformed from one form to another.
Chemical energy is the energy contained in the chemical bonds of molecules.
Radiant energy travels in waves and is sometimes called electromagnetic energy. An example is visible light.
Photosynthesis converts light energy to chemical energy.
Energy that is stored is called potential energy.
1st law- Energy cannot be created or destroyed.
cannot be created or destroyed. It can be converted from one form to
another. The sum of the energy before the conversion is equal to the
sum of the energy after the conversion.
2nd law- Some usable energy dissipates during transformations and is lost.
changes from one form of energy to another, some usable energy
dissipates, usually as heat. The amount of usable energy therefore
The energy-related reactions within cells generally involve the synthesis or the breakdown of complex organic compounds.
Anabolic reactions are those that synthesize compounds. Energy is required for these reactions.
The graph below shows that energy must be supplied to a
reaction in which covalent bonds are formed.
Reactions that break down molecules are called catabolic reactions. Energy is released when molecules are broken down.
The graph below shows that catebolic reactions break bonds and release energy.
energy in one glucose molecule is used to produce 36 ATP. ATP has
approximately the right amount of energy for most cellular reactions.
is produced and used continuously. The entire amount of ATP in an
organism is recycled once per minute. Most cells maintain only a few
seconds supply of ATP.
Nucleotides are the building blocks of nucleic acids such as DNA and RNA.
They contain a nitrogen-containing base, a 5-carbon sugar, and a
ATP is a nucleotide that contains adenine (base), ribose (sugar), and three phosphate groups.
of the molecule results in the removal of a phosphate group and the
release of energy. ATP is created by reactions that bond Pi to ADP. This reaction consumes energy; energy is stored in the ATP molecule.
Reactions that release energy are called exergonic reactions and those that require an input of energy are called endergonic reactions. Endergonic reactions do not occur spontaneously; energy must be supplied to drive the reaction.
ATP is continually produced and consumed as illustrated below.
produced by catabolic reactions provides the energy for anabolic
reactions. Anabolic and catabolic reactions are therefore coupled (they
require each other) through the use of ATP.
Substances that speed up chemical reactions are called catalysts. Organic catalysts are called enzymes.
Enzymes are specific for one particular reaction or group of related reactions.
Many reactions cannot occur without the correct enzyme present.
They are often named by adding "ase" to the name of the substrate. Example: Dehydrogenases are enzymes that remove hydrogen.
shape of the enzyme must match the shape of the substrate. Enzymes are
therefore very specific; they will only function correctly if the shape
of the substrate matches the active site.
An enzyme-substrate complex forms when the enzyme’s active site binds with the substrate like a key fitting a lock.
The product is released from the enzyme. The enzyme can be reused.
substrate molecule normally does not fit exactly in the active site.
This induces a change in the enzymes conformation (shape) to make a
In reactions that involve breaking bonds, the inexact
fit puts stress on certain bonds of the substrate. This lowers the
amount of energy needed to break them.
The enzyme does not form a chemical bond with the substrate. After the reaction, the
products are released and the enzyme returns to its normal shape.
the enzyme does not form chemical bonds with the substrate, it remains
unchanged. As a result, the enzyme molecule can be reused. Only a small
amount of enzyme is needed because they can be used repeatedly.
Activation Energy and Enzymes
In either catebolic or anabolic reactions (described earlier), additional energy must be supplied to start the reaction. This energy is called activation energy.
The amount of activation energy that is required is considerably less when enzyme is present.
Many enzymes require an additional component called a cofactor. Cofactors are not protein; they are often ions or organic molecules.
Organic cofactors are called coenzymes.
Coenzymes participate in the reaction. They may carry atoms removed from or added to the substrate or they may carry electrons.
The protein portion of the enzyme without a cofactor is inactive. It is called an apoenzyme. The complete enzyme and cofactor is called a holoenzyme.
Some important cofactors that function to carry electrons are:
NAD+ (Nicotinamide adenine dinucleotide)
NADP+ (Nicotinamide adenine dinucleotide phosphate)
FAD (Flavin adenine dinucleotide)
Rate of Reaction
with enzymes are up to 10 billion times faster than those without
enzymes. Enzymes typically react with between 1 and 10,000 molecules
Fast enzymes catalyze up to 500,000 molecules per second.
Substrate concentration, enzyme concentration, Temperature, and pH affect the rate of enzyme reactions.
lower concentrations, the active sites on most of the enzyme molecules
are not filled because there is not much substrate. Higher
concentrations cause more collisions between the molecules. With
more molecules and collisions, enzymes are more likely to encounter
molecules of reactant.
The maximum velocity of a reaction is
reached when the active sites are almost continuously filled. Increased
substrate concentration after this point will not increase the
rate. Reaction rate therefore increases as substrate
concentration is increased but it levels off.
there is insufficient enzyme present, the reaction will not proceed as
fast as it otherwise would because all of the active sites are occupied
with the reaction. Additional active sites could speed up the reaction.
the amount of enzyme is increased, the rate of reaction increases. If
there are more enzyme molecules than are needed, adding additional
enzyme will not increase the rate. Reaction rate therefore increases as
enzyme concentration increases but then it levels off.
temperature generally causes more collisions among the molecules and
therefore increases the rate of a reaction. More collisions increase
the likelihood that substrate will collide with the active site of the
enzyme, thus increasing the rate of an enzyme-catalyzed reaction.
Above a certain temperature, activity begins to decline because the enzyme begins to denature.
The rate of chemical reactions therefore increases with temperature but then decreases.
Each enzyme has an optimal pH.
A change in pH can alter the ionization of the R groups of the amino acids. When the charges on the amino acids change,
hydrogen bonding within the protein molecule change and the molecule
changes shape. The new shape may not be effective.
The diagram below shows that pepsin functions best in an acid environment. This makes sense because pepsin is an enzyme that is normally found in the stomach where the pH is low due to the presence of hydrochloric acid. Trypsin is found in the duodenum, and therefore, its optimum pH is in the neutral range to match the pH of the duodenum.
Metabolism refers to the chemical reactions that occur within cells. A hypothetical metabolic pathway is shown below.
Reactions occur in a sequence and a specific enzyme catalyzes each step.
can be used as starting points for other pathways. For example, "C" in
the diagram above can be used to produce "D" but can also be used to
metabolic pathways are cyclic. The function of the cyclic pathway below
is to produce E from A. Several intermediate steps are involved in the
production of E.
First, "A" combines with "F" to produce "B". "B"
is then converted to "C", which is then converted to "D". "D" is then
split to produce "E" (the desired product) and "F". "F" can be reused
by combining with more "A".
Regulation of Enzyme Activity
Cells have built-in control mechanisms to regulate enzyme concentration and activity.
Regulation of Protein Synthesis (Genetic Regulation)
Enzymes are proteins. You can regulate them by making more or less of them as needed. The topic of regulating protein synthesis is deferred to a later chapter.
Regulation of Enzymes Already Produced
In competitive inhibition, a similar-shaped molecule competes with the substrate for active sites.
Another form of inhibition involves an inhibitor that binds to an allosteric site of an enzyme. An allosteric site is a different location than the active site.
binding of an inhibitor to the allosteric site alters the shape of the
enzyme, resulting in a distorted active site that does not function
The binding of an inhibitor to an allosteric
site is usually temporary. Poisons are inhibitors that bind
irreversibly. For example, penicillin inhibits an enzyme needed by
bacteria to build the cell wall.
feedback inhibition is like a thermostat. When it is cold, the
thermostat turns on a heater which produces heat. Heat causes the
thermostat to turn off the heater. Heat has a negative effect on the
thermostat; it feeds back to an earlier stage in the control sequence
as diagrammed below.
enzymatic pathways are regulated by feedback inhibition. As an enzyme's
product accumulates, it turns off the enzyme just as heat causes a
thermostat to turn off the production of heat. The end product of
the pathway binds to an allosteric site on the first enzyme in the
pathway and shuts down the entire sequence.
Feedback inhibition occurs in most cells.
are molecules of RNA that function like enzymes, that is, they have an
active site and increase the rate of specific chemical reactions.
Phosphorylation refers to the chemical reactions that make ATP by adding Pi to ADP:
ADP + Pi + energy --> ATP + H2O
Phosphorylation occurs by two different kinds of reactions discussed below.
The formation of ATP in the cytoplasm is substrate-level phosphorylation.
Energy from a high-energy substrate is used to transfer a phosphate group to ADP to form ATP.
Most ATP is produced in the mitochondrion by a process that involves pumping hydrogen ions (protons) into the intermembrane space.
is required to pump hydrogen ions into the intermembrane space. The
enzyme ATP synthase is able to use the energy of this osmotic gradient to produce ATP as the hydrogen ions move by osmosis back into the matrix of the mitochondrion.
occurs in the chloroplast. The diagram below shows a chloroplast that
has been cut lengthwise to reveal the interior.
A hydrogen ion gradient is also used to produce ATP in the chloroplast (diagram below). In this case, sunlight provides energy to pump hydrogen ions into the thylakoid. The energy of their movement back into the stroma by osmotic pressure is used to produce ATP. The enzyme that uses a hydrogen ion concentration gradient to phosphorylate ADP is ATP synthase.
Photophosphorylation and oxidative phosphorylation (discussed
above) both use an osmotic concentration gradient of hydrogen ions to
produce ATP, therefore these two processes are often referred to as
Oxidation is the loss of electrons or hydrogen atoms. Oxidation reactions release energy.
Reduction is gain of electrons or hydrogen atoms and is associated with a gain of energy.
Oxidation and reduction occur together. When a molecule is oxidized, another must be reduced.
The square object in the middle diagram below represents an electron carrier. It
is capable of removing electrons or hydrogen atoms (oxidizing) from
molecules and giving them to others (reducing them).
Many enzymes require a cofactor to assist in the reaction. These "assistants" are nonprotein and may be metal ions such as magnesium (Mg++), potassium (K+), and calcium (Ca++). The cofactors bind to the enzyme and participate in the reaction by removing electrons, protons , or chemical groups from the substrate.
Cofactors that are organic molecules are coenzymes. In oxidation-reduction reactions,
coenzymes often remove electrons from the substrate and pass them to
other molecules. Often the electron is added to a proton to form a
hydrogen atom before it is passed. In this way, coenzymes serve to
carry energy in the form of electrons (or hydrogen atoms) from one
compound to another.
Vitamins are small organic molecules required in trace amounts. They usually act as coenzymes or precursors to coenzymes.
NAD (Nicotinamide Adenine Dinucleotide)
NAD+ functions in cellular respiration by carrying two electrons from one reaction site to another.
NAD+ + 2H --> NADH + H+
It oxidizes its substrate by removing two hydrogen atoms. One of the hydrogen atoms bonds to the NAD+. The electron from the other hydrogen atom remains with the NADH molecule but the proton (H+) is released. NAD+ becomes reduced to NADH.
NADH can transfer two electrons (one of them is a hydrogen atom) to another molecule.
FAD (Flavin Adenine Dinucleotide)
FAD is reduced to FADH2. It can transfer two electrons to another molecule.
FAD + 2H --> FADH2
NADH and FADH2 bring electrons to the electron transport system in cellular respiration.
Electron Carrier in Photosynthesis
NADP+ + 2H --> NADPH + H+
NADP+ is similar to NAD+ in that it can carry two electrons. One of the electrons is contained
within a hydrogen atom, the other is removed from a hydrogen atom and
the remaining proton is released..
Electrons carried by NADPH in photosynthesis are ultimately used to reduce CO2 to carbohydrate.