BIOCATALYSIS

Chapter 4

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Outline
4.1 Energy Flow in Living Things
4.2 Laws of Thermodynamics
4.3 Free Energy
4.4 Activation Energy
4.5Enzymes
4.6 Factors Affecting Enzyme Activity
4.1 Energy Flow in Living Things
 Energy - Capacity to perform work.
 Kinetic Energy - Energy of motion.
 Potential Energy - Stored energy due to an object’s relative
position.
 Thermodynamics – means “heat changes”.
 1 Kilocalorie = 1,000 calories
 Calorie - Heat required to raise temperature of 1gram of water one
degree Celsius (1°C).
 1 joule = 0.239 cal
Adrenaline or potential????
 The sun provides energy for living systems.
 Plants, algae and certain bacteria capture a fraction of this
light energy through photosynthesis.
 In photosynthesis, energy stored as potential energy in the
covalent bond between atoms in the sugar molecules.
Energy Flow in Living Things
 Oxidation-Reduction
 During a chemical reaction, the energy stored in
chemical bonds may transfer to new bonds.
 Oxidation - Atom or molecule loses an electron.
 Reduction - Atom or molecule gains an electron.
 Always take place together.
4.2 Laws of Thermodynamics
 First Law - Energy cannot be created or destroyed; it can
only change from one form to another.
 Total amount of energy in the universe remains constant.
 During energy conversion, some energy dissipates into
the environment as heat.
 Energy flows one-way from the sun through the
environment.
 Eg. The lion eating giraffe.
Laws of Thermodynamics
 Second Law - Entropy in the universe is continuously
increasing.
 States that energy which has been tranferred /
transformed will increase the entrophy of the universe.

 Entropy = A measure of the randomness or disorder of a

system; a measure of how much energy in a system has
become so dispersed (usually evenly distributed heat)
that it is no longer available to do work.
4.3 Free Energy
 Free Energy of a molecule is the amount of energy
actually available to break and subsequently form other
chemical bonds.
 Also known as the energy available to do work in any
system.
 Gibbs Free Energy : G=H-TS
 G = Gibbs Free Energy
 H = Energy contained in bonds (enthalphy)
 S = Energy unavailable due to entropy
 T = Absolute Temperature
 Free Energy
 Endergonic Reaction – Not occurs spontaneously and requires
energy input. (∆G positive)
 Exergonic Reaction - Occurs spontaneously and releases excess
free energy. (∆G negative)
Free energy (G)

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4.4 Activation Energy
 Activation Energy is the energy required to destabilize
existing chemical bonds and initiate a chemical reaction.
 Rate of exergonic reaction depends on activation energy
required for the reaction to begin.
 Catalysis - Process of lowering necessary activation
energy. Eg. enzyme
 Activation Energy and Catalysis
Free energy (G)

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4.5 Enzymes
 Enzymes carry out most catalysis in living organisms.
 Unique three-dimensional shape of an enzyme enables it
to stabilize a temporary association between substrates.
 Lowers activation energy necessary for new bonds to
form.
 The enzymes itself is not changed or consumed in the
reaction, can be used over and over.
 Eg. Carbonic anhydrase (enzyme in RBC)
Enzymes
 How Enzymes Work
 Most enzymes are globular proteins with one or more
pockets or clefts, called active sites for substrates to
bind.
 Substrate molecules must fit precisely into an active site.
 Amino acids side group of enzyme end up very close to
certain bonds of the substrate.
 These groups interact chemically with the substrate,
usually stressing or distorting a particular bond and
consequently lowering the activation energy needed to
break the bond.
 After the bonds of the substrates are broken, new bonds
are formed, the substrates have been converted to
products.
 Products dissociate from the enzyme.
 The enzyme ready to binds its next substrate and begin
the cycle again!..
Enzyme Catalytic Cycle

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Enzymes
 Enzyme Forms
 Multienzyme Complexes
 Enzymes catalyzing different steps of a sequence are
loosely associated with one another.
 Increase catalytic efficiency.
 Eg. The bacterial pyruvate dehydrogenase.
 Not all Biological Catalysts are Proteins. Some are
actually RNA molecules called ribozymes.
4.6 Factors Affecting Enzyme Activity
 Temperature
 Rate increase with temperature up to temperature
optimum. (37 °C- 40°C)
 As temperature increase, more atoms which make up the
enzyme molecules vibrate.
 Temperature above 40 °C breaks the bonds such as
hydrogen bonds, ionic bonds which hold the molecules
in their precise shape.
 The enzyme may be denaturated, that is complete loss of
normal three dimensional shape at high temperature.
 pH
 Changing concentration of hydrogen ions shifts the
balance between positively and negatively charged amino
acid residues.
 Optimum pH that usually ranges from pH 6 to 8.
 At optimum pH the enzyme functions most efficiently.
 pH 2 = pepsin
 pH 8 = trypsin
Factors Affecting Enzyme Activity
 Inhibitors and Activators
 Inhibitors - Decrease enzyme activity.
 Competitive - Compete with substrate for same
binding site.
 Noncompetitive - Bind to enzyme in other location,
altering shape.
 Allosteric Site
 Activators - Bind to allosteric sites and keep enzymes in
active configurations.
 Increase enzyme activity.
Factors Affecting Enzyme Activity
 Enzyme Cofactors - Enzyme function assisted by
additional chemical components.
 Eg. Metallic ion zinc, molybdenum, manganase.

 Coenzyme – cofactor is a nonprotein organic molecules.

 Eg. Vitamin B6 and B12.
ATP
 Adenosine triphosphate (energy currency)
 Composed of:
 Five-carbon sugar (ribose)
 Adenine
 Triphosphate group
 Energy Storage
 Phosphate groups are highly negatively charged.
 Unstable bonds easily broken.
ATP
 Cells use ATP to drive endergonic reactions.
 Instability makes ATP ideal for short-term energy
source, but a poor candidate for long-term energy
storage.
Biochemical Pathways
 Metabolism - Total of all chemical reactions carried out
by an organism.
 Anabolism – required energy to build up molecules.
 Catabolism – released energy to break down
molecules.
 Biochemical Pathways - Products of one reaction
becomes substrate for the next.
 Regulated by feedback inhibition.
Biochemical Pathways
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