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Living systems decrease their entropy by increasing

the molecular orderliness of their structure

. Life is a constant flow of energy.

All life¶s processes are guided by chemical reactions
which would either require or release energy
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A. 
   



1. The increase in the molecular orderliness of living systems

appears to contradict the second law of thermodynamics.
2. However, in order to increase its molecular orderliness,
it reduces the molecular orderliness of a much larger
amount of food.
3. Continuous provision of additional food is only possible
from the sun¶s continual input.
4. Eventually the orderly structure of the organism will end
at death; entropy wins out.
5. Cellular metabolism is the collective total chemical
processes that maintain living cells
The process of cellular respiration
harvest the energy in food and
converts it into ATP that is needed
to power biological functions.

Through photosynthesis, plants

convert the energy stored within it
into chemical energy
V 




1. Energy exists in two states.

a. 


 is energy of motion.
b. 
 

 is stored energy; it is not doing work
but has the capacity to do work.
2. The two laws of thermodynamics govern conversion of
energy from one form to another.
a. First law of thermodynamics: energy cannot be created
or destroyed but it can be changed from one form
to another.
b. Second law of thermodynamics: a closed system moves
toward increasing disorder or entropy but living systems
maintain and increase their organization as energy
enters from the sun
Energy and the Laws of Thermodynamics

Definition of Energy
Energy is the capacity to do work.

Kinds of Energy
1. Kinetic energy - energy in motion
e.g. light energy (movement of photons)
heat energy ( movement of molecules)
electricity (movement of electrically charged
particles)
2. Potential energy - stored energy
chemical energy stored in bonds
electrical energy stored in battery
energy stored in a diver about to dive
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1. Energy cannot be created nor destroyed, it can only be

changed from one form to another
known as the ³Law of Conservation of Energy
e.g. burning of wood

2. There is no loss of total energy, but there is a loss of

useful energy

Entropy - tendency toward loss of orderliness and

and an increase in randomness, disorder and
low-level energy
=
 


_ 



 is the amount of energy that is free
to do work after a chemical reaction; it is energy present
in chemical bonds minus energy that cannot be used.
4. In cells, most reactions are



that release free energy; they are spontaneous and
proceed ³downhill.´
5. In cells, some important reactions are



that require free energy; they must be ³pushed uphill.´
6. ATP is an important molecule that powers many
endergonic reactions
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A.  
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1. In any reaction, exergonic or endergonic, chemical bonds
must be destabilized for the reaction to proceed.
2. Activation energy must be provided to break a bond;
this is done by catalysts or by raising the temperature.
3. Enzymes are catalysts that reduce the amount of
activation energy required for a reaction, making it more
likely but not altering the change in free energy.
B. ! 
 

1. Enzymes vary from small to large molecules;
some are pure proteins.
2. Some enzymes require nonprotein   to perform
enzymatic functions.
3. Organic cofactors are called 
 
; they are derived
from vitamins in the diet.
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1. Enzymes are proteins which carry out the catalysis

in living organisms.
Every enzyme is specific in its action; it has a unique
molecular configuration and active site to catalyze
only one specific reaction.
2. A  
is a reactant in an enzymatic reaction.
-the molecules that wil undergo the reaction
3. The enzyme binds to substrate to form an

 
" 
 
 for a brief moment.
4. Proof of the brief enzyme-substrate complex state is that
at high substrate concentration, all catalytic sites may be
filled for a brief time.
5. Conversion of glucose to carbon dioxide requires
19 reactions, each with a specific enzyme.
How Enzymes Work

Enzymes have active sites wherein substrates bind

Active sites ± packets or clefts on the surface of

enzymes
A substrate molecule must fit
precisely into an active site.

When that happens, amino acid

side groups of the enzyme end
up in close proximity to certain
bonds of the substrate.
The side groups interact chemically
with the substrate, usually stressing
or distorting a particular bond,
and consequently lowering the
activation energy needed
to break the bond

.The substrate, now a product,

dissociate from the enzyme
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1. Specificity of enzyme and substrate means that no

useless by-products are formed.
2. Most enzymes take on only one substrate at a
time; a few will act on many proteins.
3. Some enzymes will repeat the catalysis billion of
times until worn out.
4. Some enzymes undergo catalytic cycles at speed
of a million cycles per minute.
High specificity of trypsin. It splits only peptide bonds adjacent to lysine
or arginine.
  
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1. Enzyme-catalyzed reactions are reversible but most

reactions are in one direction.
2. Some enzymes degrade proteins (catabolism) and
other enzymes synthesize them (anabolism).
3. Net direction of a chemical reaction depends on
relative energy contents of substances involved.
4. Many enzymes are repeatedly activated and
inactivated and several mechanisms for regulating
enzyme activities are well known.
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ATP formation from ADP and AMP
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A. |


1. Coupled reactions occur when energy released by an
exergonic reaction is used to drive an endergonic reaction.
2. Energy released from ATP ±±±±> ADP + P is central to
many biological reactions.
3. ATP breakdown is coupled to a reaction that requires
energy; both reactions take place at the same time
in the same place.
4. The bond energy released in the reaction is transferred
to ADP + P which becomes ATP.
5. ATP is an energy-coupling agent and not a fuel; it is formed
as needed and therefore metabolism is mostly
self-regulating.
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1. All cells obtain their chemical energy requirements from
oxidation-reduction reactions.
2. In oxidation-reduction (redox) reactions, electrons pass
from one molecule to another.
3. #  is the loss of electrons.
4. 
 is the gain of electrons.
5. Both reactions occur at the same time because one
molecule accepts electrons given up by another molecule.
6. When the oxidized agent accepts electrons, energy is
liberated as electrons move to a more stable position.
7. As electrons move through a series of carriers, each carrier
is reduced by accepting electrons and reoxidized by
passing electrons to the next carrier.
8. Gradual release of energy ensures a maximum yield of ATP.
9. Electrons are ultimately transferred to a final electron acceptor.
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1. Oxygen is the final electron acceptor in aerobes

2. Anaerobic metabolism employs some other final
electron acceptor.
3. Evolution has favored aerobic metabolism because it
is more efficient.
4. Complete oxidation of glucose releases nearly 20
times more energy; therefore less food is required to
maintain metabolism.
| #



 

1. Oxidation of fuel molecules is removal of electrons,

not direct combination of oxygen with fuel.
2. Hans Krebs described three stages of complete oxidation
of fuel molecules.
3. Stage I -digestion, the breakdown of large molecules to
smaller ones in intestinal tract, does not yield useful
energy.
4. In Stage II, also known as glycolysis, most foodstuffs
are degraded into two 3-carbon units (pyruvic acid),
but little ATP is generated.
5. In Stage III, food undergoes final oxidation until electrons
are accepted by molecular oxygen to form water,
with a large yield of ATP.
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1. Addition of two phosphate groups activates glucose.

2. Two separate reactions use two ATP.
3. Glucose, a C6 molecule, splits into two C3 (pyruvic
acid) fragments.
4. Two electrons and one hydrogen ion are accepted by
NAD+ and result in two NADH.
5. Enough energy is released from breakdown of glucose
to generate four ATP molecules.
6. Two of four ATP molecules produced are required to
replace two ATP molecules used in the
phosphorylation of glucose.
7. There is a net gain of two ATP from glycolysis.
8. Glucose + 2ADP + 2Pi + 2NAD+ ±±±±> 2 pyruvic acid +
2NADH + 2ATP
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1. The two molecules of pyruvic acid enter a mitochondrion.

2. Each is oxidized; one molecule of carbon dioxide is
released.
3. The 2-carbon residue condenses with coenzyme A to
form acetyl coenzyme A (acetyl-CoA).
 
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1. Degradation of the 2-carbon acetyl group of acetyl-CoA

occurs in the Krebs cycle.
2. Acetyl coenzyme A condenses with a 4-carbon acid
releasing coenzyme A to react again.
3. A series of reactions releases the two carbons as
carbon dioxide; oxaloacetic acid is regenerated.
4. Hydrogen ions and electrons in the oxidations are
transferred to NAD and FAD; a pyrophosphate bond
is generated in guanosine triphosphate.
5. The high-energy phosphate transfers to ADP to form
ATP.
6. Acetyl unit + 3NAD+ + FAD + ADP + Pi ±±±±> 2CO2 +
3NADH + FADH2 + ATP
7. 11 molecules of ATP are formed; other molecules are
reactants and recycled products.
 
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1. High-energy electrons are delivered to the protein-

based system and low-energy electrons leave it.
2. The H+ gradient produced drives the synthesis of ATP.
3. Reduced FAD from the Krebs cycle enters the electron
transport chain at a lower level than NADH and yields
two ATP molecules.
4. ATP production is tied to a proton (H+) gradient across
membranes; this is called chemiosmotic coupling.
4 
# 
   

1. Glucose + 2 ATP + 36 ADP + 36 P + 6 O2 ±±±±>

6 CO2 + 2 ADP + 36 ATP + 6 H2O
2. Cytoplasmic NADH from glycolysis requires one molecule
of ATP to fuel transport of each NADH into mitochondria.
3. Net yield may be as high as 36 molecules of ATP
per glucose molecule.
4. Efficiency of aerobic oxidation is 38%; human-designed
systems seldom exceed 5±10% efficiency.
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1. In absence of molecular oxygen, oxidation of pyruvic acid cannot occur.

2. Most animals therefore reduce pyruvic acid to lactic acid, which
becomes the final electron acceptor.
3. In alcoholic fermentation, one pyruvic acid carbon is released as
carbon dioxide and the resulting 2-carbon compound is reduced to
ethanol.
4. This provides some high-energy phosphate in situations where oxygen
is depleted.
5. Animals reduce pyruvate to lactate when it is produced faster than the
Krebs cycle can oxidize it.
6. When blood cannot remove all of the lactate from muscles, the lactate
changes pH and causes muscles to fatigue and the animal is in


 because oxygen is still needed after exercising.
7. Diving birds and salmon need muscular bursts in the absence of
oxygen.
8. Some parasitic animals have dispensed with oxidative phosphorylation
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1. The first step in breakdown of a triglyceride is

hydrolysis of glycerol and fatty acid molecules.
2. Glycerol is phosphorylated and enters the
glycolytic pathway.
3. The remainder is fatty acids; stearic acid is common.
4. Long hydrocarbon chains are sliced by oxidation of two
carbons at a time.
5. Complete oxidation of one stearic acid nets 146 ATP
molecules; glucose yielded 108 ATP molecules.
V  


1. Fat stores are concentrated fuels.

2. Fats contain almost pure hydrocarbons.
3. Acetyl coenzyme A is a source of carbon atoms to
build fatty acids; carbohydrates, fats, and proteins
that can be degraded to acetyl coenzyme A.
4. Most usable fat is in adipose tissue; women average
30% more fat than men.
5. Many researchers are now investigating the
physiological and psychological aspects of obesity.
6. There is increasing evidence that food intake and
feeding centers located in the brain regulates the
amount of fat deposition.
7. There is also evidence that there is a genetic
composition to obesity.
þ

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A. = =
1. Each of the 20 amino acids requires a separate pathway
for synthesis and degradation.
2. Tissues use the amino acid pool, in the blood and
extracellular fluid, as a source of molecules.
3. Excess proteins serve as fuel just like carbohydrates
and fats; carnivores get nearly half of their high-energy
phosphate from amino acid oxidation.
4. Nitrogen is removed from amino acids by deamination;
carbon skeletons then enter regular routes of metabolism.
5. The other product of deamination is toxic ammonia;
aquatic animals excrete it directly but terrestrial animals
must convert it to less toxic urea or uric acid.
6. Uric acid is insoluble allowing removal in solid form;
desert animals that need to conserve water use it.
þ
 
þ

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A. Many enzymes act reversibly: synthesis or degradation

results in balance.
B. If an enzyme converts A to B and B is removed,
the enzyme will tend to restore the ratio of B to A.
C. Genes may switch enzymes on or off; some molecules
alter the shape of enzymes, and enzymes may have
active and inactive forms.
þ