ENERGY AND

METABOLISM
BIO 01

THIS REVIEWER IS BASED ON THE GIVEN .PPT FROM THE BLACKBOARD

MAPUA SHS – SCIENCE CLUB

BIO01 Credits to Sir. Christian Tan and the Science Club

Energy and Metabolism

Chapter 6
Impacts, Issues:

A Toast to Alcohol Dehydrogenase

- In the liver, alcohol dehydrogenase helps break down toxic alcohols, but at the expense
of liver function and energy metabolism

Alcohol dehydrogenase

- This enzyme, which helps the

body break down ethanol and
other toxic alcohols, makes it
possible for humans to drink
beer, wine, and other
alcoholic beverages.

Flow of Energy

 Energy: the capacity to do work

- kinetic energy: the energy of motion
- potential energy: stored energy
 Energy can take many forms: chemical, mechanical, electric current, heat, light
 Most forms of energy can be converted to heat energy.
 Heat energy is measured in kilocalories.
 One calorie = the amount of heat required to raise the temp of water by 1 oC.

1 kilocalorie (kcal) = 1000 calories (Cal.)

Laws of Thermodynamics

First Law of Thermodynamics

- energy cannot be created or destroyed
- energy can only be converted from one form to another

For example:
sunlight energy - - - -  chemical energy
photosynthesis

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BIO01 Credits to Sir. Christian Tan and the Science Club

Second Law of Thermodynamics:

- disorder is more likely than order

Entropy: disorder in the universe

 The 2nd Law of Thermodynamics states

that entropy is always increasing.

 Energy is required to keep order, to do

work.
- keep cells together and organized
- perform life processes

Enthalpy: All the energy contained in a

molecule’s chemical bonds

 Free energy: the energy available to do work, to reduce disorder (enthalpy)

- denoted by the symbol G (Gibb’s free energy)
 free energy = enthalpy – (entropy x temp.)
G = H - TS
 Chemical reactions can create changes in free energy:
G =  H - T  S
 When products of chemical reactions contain more free energy than reactants – G is
positive.
 When reactants contain more free energy than products – G is negative.
 Chemical reactions can be described by the transfer of energy that occurs:

Endergonic Reaction: a reaction requiring an input of energy

  G is positive
Exergonic Reaction: a reaction that releases free energy
 G is negative

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BIO01 Credits to Sir. Christian Tan and the Science Club

 Most reactions require some energy to get started ─ activation energy

Activation Energy: extra energy needed to get a reaction started:

- destabilizes existing chemical bonds
- required even for exergonic reactions

Catalysts: substances that lower the activation energy of a reaction (enzymes)

 Potential energy stored in chemical bonds can be transferred from one molecule to
another by way of electrons.
oxidation: loss of electrons
reduction: gain of electrons

 Redox reactions are coupled to each other.

Oxidation-Reduction Reactions
- A chemical reaction that transfers electrons from one
atom to another
Oxidation = loss of an electron
Reduction = gain of an electron

Oxidation

- A chemical reaction in which a molecule gives up electrons.

- Oxidation releases energy
- The molecule losing the electron is oxidized.

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Reduction
- A chemical reaction in which a molecule gains electrons and energy.
- The molecule that accepts electrons is reduced.
- The molecule being reduced receives energy.

LEO the lion says GER

- If it Loses Electrons during the reaction, it’s Oxidized.
- If it Gains Electrons during the reaction, it’s Reduced.

Redox Reactions
 Oxidation and Reduction reactions always occur in pairs
- If an atom or molecule is reduced, another atom or molecule must have been
oxidized.
- If an atom or molecule is oxidized, another atom or molecule must have been
reduced.
 For this reason, Oxidation and Reduction Reactions are known as Redox Reactions.

ATP - Energy Currency of Cells

 ATP is the molecule that cells use to store, transfer, and provide energy.
 The energy from ATP is used to fuel anabolic reactions
- recall: for growth, repair, and reproduction
ATP = Adenosine Triphosphate
Adenosine (same molecule from DNA and RNA)
+
Three inorganic phosphates (functional group PO4)

 ATP = adenosine triphosphate

- the energy “currency” of cells

 ATP structure:
- ribose, a 5-carbon sugar
- adenine
- three phosphates

o ATP - 1 PO4 = ADP (Adenosine

Diphosphate)

o ADP - 1 PO4 = AMP (Adenosine

Monophosphate)

o ADP + 1 PO4 = ATP

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BIO01 Credits to Sir. Christian Tan and the Science Club

ATP

ATP
 ATP is a molecule that is used as an Energy Currency in cells

- ATP’s can be broken down to provide energy for endergonic reactions.

- Cells use energy to build ATP’s
- Enzymes of allow cells to efficiently build ATP’s - Cells can make ATP’s for less energy
than ATP’s can provide.

 ATP stores energy in the covalent bonds between phosphates:

- Phosphates are highly negative, therefore:

o the phosphates repel each other.
o much energy is required to keep the phosphates bound to each other.

 Energy is released when the bond between two phosphates is broken.

o When the bond between phosphates is broken:
ATP - - - - - - - - ADP + Pi
energy is released

o ADP = adenosine diphosphate

o Pi = inorganic phosphate ○ This reaction is reversible...

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ATP/ADP Cycling

 When the bond between phosphates is formed:

ADP + Pi ATP
energy is consumed

ATP - ADP Cycle

 It costs energy to build ATPs

ADP + 1P ATP
(Adenosine Diphosphate + 1 phosphate)

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Energy Currency of Cells

- The energy released when ATP is broken down to ADP can be used to fuel endergonic
reactions.
- The energy released from an exergonic reaction can be used to fuel the production of
ATP from ADP + Pi.

Other Functions of ATP

- ATP regulates enzyme activity

- Phosphorylation and dephosphorylation - process of adding or removing phosphate
groups - can activate or deactivate enzymes.
- ATP serves as a source of phosphate groups.

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BIO01 Credits to Sir. Christian Tan and the Science Club

Enzymes

- Molecules that catalyze - speed up - biochemical reactions in living cells

- Three rules to be considered an enzyme
 Most are proteins (some RNA enzymes)
 Lower the energy of activation required for a reaction to occur.
 Are not changed or consumed by the reaction.
- Cofactors, Coenzymes

Metabolism
 Enzymes catalyze cellular chemical reactions
 Metabolism - the chemical reactions in a cell.
 Two categories of cellular chemical reactions:
1. Anabolic Reactions
 Build larger molecules for growth, repair, reproduction
 Dehydration Synthesis Reactions
 Require energy and nutrients
2. Catabolic Reactions
 Breakdown larger molecules
 Hydrolysis Reactions
 Mobilize nutrients for energy making it available to the cell.
 Metabolism is the sum of all anabolic and catabolic reactions that occur in the cell

 The metabolism of cells is carried out and controlled by the enzymes

- There are catabolic enzymes – those that cleave larger molecules into smaller ones.
Ex. Hydrolysis Reactions
- There are also anabolic enzymes – those that assemble smaller molecules into
larger ones.
Ex. Dehydration Reactions
Enzymes
Enzymes interact with substrates.

Substrate
- Molecule that will undergo a reaction when bound to the enzyme.
- lactose, hydrogen peroxide (H2O2)

On the Enzymes:
- Active site: region of the enzyme that binds to the substrate.
- Allosteric site: region of the enzyme that binds substances other that the substrate.

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 Binding of an enzyme to a
substrate causes the
enzyme to change shape,
producing a better
induced fit between the
molecules.

Enzymes
 Enzymes are very specific:
- Enzymes will only interact with specific substrates.
- The substrate fits into the active site like a key fit into a lock. (Lock and Key
Hypothesis)
- Substrate binding causes the
enzyme to change shape,
producing a better induced fit
between the molecules.
(Induced Fit Hypothesis)

 Changing the shape of an enzyme

affects its ability to function.
 Enzyme/Substrate Complex:

E+S ES EP E+P

1. The Enzyme and the Substrate come together (E+S)

2. The Enzyme/Substrate Complex is formed (ES)
3. The Enzyme’s Substrate is changed to the Enzyme’s
- Product in the active site of the enzyme (EP)
4. The Enzyme and Product Separate (E+P)
5. The Enzyme is free to bind to another substrate.

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BIO01 Credits to Sir. Christian Tan and the Science Club

Enzyme Naming Convention

 Because enzymes catalyze specific reactions each enzyme has a unique name:
- The first part of an enzyme’s name usually describes the substrate.
- The second part of an enzymes usually indicates the type of reaction it will catalyze.
 Most enzyme names end in the suffix -ase
 Examples of Enzymes:
- DNA polymerase
- Glycogen synthetase
- Lactase
- Catalase

How Enzymes Work

 Enzymes lower the activation energy of biochemical reactions.
 Enzymes make it easier for chemical reactions to occur:
- by destabilizing the bonds in
the substrate
- by bringing substrates
together so they react
- by decreasing entropy -
disorder - in the system
 Enzymes make the chemical
reactions possible in the cell’s
environment.
 Enzymes make cells very
efficient.

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Enzymes make cells very efficient

 Through enzymes, cells can carry out anabolic and catabolic reactions and end up with a
net profit of energy.
 Cellular respiration is the process of breaking down glucose and storing the excess energy
from the molecule into a form of energy that is available and useful to the cell.

Cells Use Enzymes to Process Energy and Matter

 Reactions that break chemical bonds release
their internal potential energy.
- Example: burning wood
- Oxidation reactions
 Organisms obtain energy through enzyme-
catalyzed biochemical reactions.

Coenzymes and Cofactors

 Many enzymes require special molecules to help them function correctly:
- Cofactors
 inorganic molecules ions, such as zinc or iron
- Coenzymes
 organic molecules
 Vitamins are the precursors for many coenzymes.
 Vitamins must be acquired from the diet; cells cannot make them.

The Role of Coenzymes

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The Environment Affects Enzyme Function

 The rate at which an enzyme can bind to a substrate is called the turnover number.
 The turnover number is maximized under the ideal conditions for that enzyme.
 Conditions that can change an enzyme’s 3-dimensional shape can change its function.
 Each enzyme has ideal conditions that include:
a) Temperature
b) pH
c) Substrate concentration
d) Regulatory molecules

Temperature
 Temperature has two effects on enzymes:
I. Changes the rate of molecular motion
- Increasing temperature increases molecular
motion and increases turnover number.
- Decreasing temperature decreases
molecular movement and decreases
turnover number.
II. Causes changes in the shape of an enzyme
- Temperature changes above optimum will
denature the enzyme.
- This changes its shape, and it can no longer
bind substrate and catalyze the reaction.

pH
 Enzymes are composed of amino acids
- In a basic environment
 The acidic side chains (R groups) could
donate protons which affects the charge of
the side chain.
 A neutral side chain that donates protons
would become negatively charged.
- In an acidic environment
 The basic side chains (R groups) could
accept protons which affects the charge of
the side chain.
 A neutral side chain that accepts
protons would become positively
charged.

 Both events can change the enzyme’s

shape.

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 Enzymes work together in chains of

reactions known as biochemical or
metabolic pathways.
 Biochemical pathways are a series of
reactions in which the product of one
reaction becomes the substrate for the
next reaction.
 Examples: photosynthesis, cellular
respiration, protein synthesis, etc.

Metabolic Pathways
 Metabolic Pathways are series of
chemical reactions carried out by
separate enzymes.
 It is a sequence of chemical reactions
where each reaction is controlled by a
separate enzyme.
 The product of one enzyme serves as the
substrate for the enzyme of subsequent reaction in the metabolic pathway.
 These biochemical pathways offer certain advantages:
- The product of one reaction can be directly delivered to the next enzyme.
- The possibility of unwanted side reactions is eliminated.
- All the reactions can be regulated.

Regulation of Biochemical Pathways

 Metabolism is tightly regulated
 There is a delicate balance between all
the reactions that take place in the
cell.
 Metabolism is commonly regulated 3
ways:
- Enzymatic competition for
substrate
- Gene regulation
- Enzyme inhibition

Enzyme Regulation
A. Enzymatic Competition for Substrate
 Enzymatic competition occurs
when more than one enzyme
interacts with the same substrate.
 Each enzyme converts the substrate to a different product.
 The enzyme that “wins” is the one that is the most abundant at the time.

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B. Gene Regulation
 Enzymes are proteins.
 Protein production is controlled by genes.
 Certain chemicals in the cell turn enzyme-producing genes on or off depending on
the situation.
- Called gene-regulator proteins
o Those that decrease the amount of an enzyme made are called gene-
repressor proteins.
o Those that increase the amount of an enzyme made are called gene-
activator proteins.
C. Enzyme Inhibition
 Inhibitors are molecules that attach to enzymes and make them unable to bind to
substrate.
 Many drugs, pesticides and herbicides target enzymes.
 Three types of Inhibition:
- Negative Feedback Inhibition
- Competitive Inhibition
- Noncompetitive Inhibition
I. Negative-Feedback Inhibition
 The end-product of the metabolic pathways accumulate
- Those molecules feedback and bind to an enzyme early in the sequence.
- They inhibit that enzyme, and stop the sequence.
- This decreases the amount of end-product made.
 This functions to keep levels of the end-product within a certain range.

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 Inhibitors are molecules that bind to an enzyme to decrease enzyme activity.

- Competitive Inhibitors compete with the substrate for binding to the same
active site.
- Noncompetitive Inhibitors bind to sites other than the enzyme’s active site.
III. Competitive Inhibition
 Competitive inhibitors closely resemble the substrate.
- They bind to the active site of the enzyme and block the substrate from binding.

 Allosteric enzymes exist in either an active or inactive state.

- Possess an allosteric site where molecules other than the substrate bind.
- Allosteric Inhibitors bind to the allosteric site to inactivate the enzyme.
- Allosteric Activators bind to the allosteric site to activate the enzyme.
IV. Noncompetitive Inhibition
 Noncompetitive inhibitors bind to sites other than the enzyme’s active site -
allosteric sites
 “allo” = other; “steric” =
shape
- Binding to an allosteric
site changes the shape
of the enzyme and
affects its function.
 Noncompetitive because
the noncompetitive
inhibitor does not compete
with the substrate to bind
to the active site.

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Cellular Respiration
 Cellular Respiration is a metabolic pathway that breaks down glucose and extracts the
energy to produce energy.
C6H12O6 + 6O2 6H2O + 6CO2 + Energy
Glucose Oxygen Water Carbon Dioxide

 The Energy is in the form of ATP

 Glucose contains energy that can be extracted
 Cellular Respiration is a metabolic pathway that breaks down glucose and extracts the
energy to produce ATP.
 Recall:

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