Madam Syakira

ENZYMES
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Page 1
Overview: The Energy of Life

The living cell is a miniature chemical factory where thousands of reactions occur The cell extracts energy and applies energy to perform work Some organisms even convert energy to light, as in bioluminescence
Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Page 2
An organisms metabolism transforms matter and energy, subject to the laws of thermodynamics
Metabolism is the totality of an organisms chemical reactions Metabolism is an emergent property of life that arises from interactions between molecules within the cell
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Organization of the Chemistry of Life into Metabolic Pathways
A metabolic pathway begins with a specific molecule and ends with a product Each step is catalyzed by a specific enzyme
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Enzyme 1
Enzyme 2 B C Reaction 2
Enzyme 3 D Reaction 3
A
Reaction 1
Starting molecule
Product
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Catabolic pathways release energy by breaking down complex molecules into simpler compounds Cellular respiration, the breakdown of glucose in the presence of oxygen, is an example of a pathway of catabolism
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Anabolic pathways consume energy to build complex molecules from simpler ones The synthesis of protein from amino acids is an example of anabolism Bioenergetics is the study of how organisms manage their energy resources
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Forms of Energy
Energy is the capacity to cause change Energy exists in various forms, some of which can perform work
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Kinetic energy is energy associated with motion Heat (thermal energy) is kinetic energy associated with random movement of atoms or molecules Potential energy is energy that matter possesses because of its location or structure
Chemical energy is potential energy available for release in a chemical reaction

Energy can be converted from one form to another
A diver has more potential energy on the platform than in the water.
Diving converts potential energy to kinetic energy.
Climbing up converts the kinetic energy of muscle movement to potential energy.
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A diver has less potential energy in the water Powerpoint than Templates on the platform.
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Thermodynamics is the study of energy transformations A closed system, such as that approximated by liquid in a thermos, is isolated from its surroundings In an open system, energy and matter can be transferred between the system and its surroundings Organisms are open systems
The Laws of Energy Transformation
According to the first law of thermodynamics, the energy of the universe is constant:
Energy can be transferred and transformed, but it cannot be created or destroyed
The First Law of Thermodynamics
The first law is also called the principle of conservation of energy
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During every energy transfer or transformation, some energy is unusable, and is often lost as heat According to the second law of thermodynamics:
Every energy transfer or transformation increases the entropy (disorder) of the universe
The Second Law of Thermodynamics
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Heat
Chemical energy
CO2 + H2O
(a) First law of thermodynamics
(b) Second law of thermodynamics
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Living cells unavoidably convert organized forms of energy to heat Spontaneous processes occur without energy input; they can happen quickly or slowly For a process to occur without energy input, it must increase the entropy of the universe
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Biological Order and Disorder

Cells create ordered structures from less ordered materials Organisms also replace ordered forms of matter and energy with less ordered forms Energy flows into an ecosystem in the form of light and exits in the form of heat
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The evolution of more complex organisms does not violate the second law of thermodynamics Entropy (disorder) may decrease in an organism, but the universes total entropy increases
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The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously
Biologists want to know which reactions occur spontaneously and which require input of energy To do so, they need to determine energy changes that occur in chemical reactions
Free Energy and Metabolism

The concept of free energy can be applied to the chemistry of lifes processes
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An exergonic reaction proceeds with a net release of free energy and is spontaneous An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous
Exergonic and Endergonic Reactions in Metabolism
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Fig. 8-6 Reactants Free energy Amount of energy released (G < 0)
Energy
Products
Progress of the reaction (a) Exergonic reaction: energy released Products Free energy Amount of energy required (G > 0)
Energy
Reactants
Progress of the reaction (b) Endergonic reaction: energy required Free Powerpoint Templates
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Fig. 8-6a
Reactants
Amount of energy released (G < 0)
Energy
Free energy
Products
Progress of the reaction (a) Exergonic reaction: energy released

Fig. 8-6b
Products
Free energy
Amount of energy required (G > 0)

Energy
Reactants
Progress of the reaction
(b) Endergonic reaction: energy required

Equilibrium and Metabolism

Reactions in a closed system eventually reach equilibrium and then do no work Cells are not in equilibrium; they are open systems experiencing a constant flow of materials
A defining feature of life is that metabolism is never at equilibrium

A catabolic pathway in a cell releases free energy in a series of reactions
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ATP powers cellular work by coupling exergonic reactions to endergonic reactions

A cell does three main kinds of work: Chemical Transport Mechanical To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one Most energy coupling in cells is mediated by ATP
ATP (adenosine triphosphate) is the cells energy shuttle ATP is composed of ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups
The Structure and Hydrolysis of ATP
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Fig. 8-8
Adenine
Phosphate groups Ribose
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The bonds between the phosphate groups of ATPs tail can be broken by hydrolysis Energy is released from ATP when the terminal phosphate bond is broken This release of energy comes from the chemical change to a state of lower free energy, not from the phosphate bonds themselves
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Fig. 8-9
Adenosine triphosphate (ATP)
H2O
Pi
Energy
Inorganic phosphate
Adenosine diphosphate (ADP)

How ATP Performs Work

The three types of cellular work (mechanical, transport, and chemical) are powered by the hydrolysis of ATP In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction Overall, the coupled reactions are exergonic
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ATP drives endergonic reactions by phosphorylation, transferring a phosphate group to some other molecule, such as a reactant The recipient molecule is now phosphorylated
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Fig. 8-11
Membrane protein
Pi
Solute
Solute transported
ADP
+ P
(a) Transport work: ATP phosphorylates transport proteins ATP
Vesicle
Cytoskeletal track
ATP
Motor protein
Protein moved
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(b) Mechanical work: ATP binds noncovalently to motor proteins, then is hydrolyzed Free Powerpoint Templates
The Regeneration of ATP

ATP is a renewable resource that is regenerated by addition of a phosphate group to adenosine diphosphate (ADP) The energy to phosphorylate ADP comes from catabolic reactions in the cell The chemical potential energy temporarily stored in ATP drives most cellular work
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Fig. 8-12
ATP + H2O
Energy from catabolism (exergonic, energy-releasing processes)
ADP + P i
Energy for cellular work (endergonic, energy-consuming processes)
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Enzymes
1. 2. 3. 4. Enzymes speed up metabolic reactions by lowering energy barriers Enzymes are substrate specific The active site in an enzymes catalytic center A cells physical and chemical environment affects enzyme activity
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1. Enzymes speed up metabolic reactions by lowering energy barriers

A catalyst is a chemical agent that changes the rate of a reaction without being consumed by the reaction.
An enzyme is a catalytic protein.
Enzyme: An organic catalyst (usually protein) that accelerate a specific chemical reaction by lowering the activation energy required for that reaction.
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Anabolism: Aspect of metabolism simpler substances are combined to form complex substances for storage of energy for the production of new cellular materials and growth. Catabolism: Aspect of metabolism complex substances are broken down to simpler substance releasing chemical energy. Metabolism = Catabolism + Anabolism
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Exergonic reaction: release of energy.
Endergonic reaction Absorb energy.
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Chemical reactions between molecules involve both bond breaking and bond forming.
To hydrolyze sucrose, the bond between glucose and fructose must be broken and then new bonds formed with a hydrogen ion and hydroxyl group from water.
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In an exergonic reaction, the reactants must still absorb energy from the surroundings, the activation energy (EA), to break the bonds.
This energy makes the reactants unstable, increases the speed of the reactant molecules, and creates more powerful collisions.
In exergonic reactions, the activation energy released back to the surroundings, more energy is released with the formation of new bonds.
Activation energy is the amount of energy necessary to push the reactants over an energy barrier.
At the summit the molecules are at an unstable point, the transition state. The difference between free energy of the products and the free energy of the reactants is the delta G.
For some processes, the barrier is not high and the thermal energy provided by room temperature is sufficient to reach the transition state. In most cases, EA is higher and a significant input of energy is required.
A spark plug provides the energy to energize gasoline. Without activation energy, the hydrocarbons of gasoline are too stable to react with oxygen.
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The laws of thermodynamics would seem to favor the breakdown of proteins, DNA, and other complex molecules.
However, in the temperatures typical of the cell there is not enough energy for a vast majority of molecules to make it over the hump of activation energy. Yet, a cell must be metabolically active. Heat would speed reactions, but it would also denature proteins and kill cells.
Denature: To alter the physical properties and three dimensional structure of protein, usually by treating it with excess heat, strong acid or strong base. Reactant: substrate that participate in a chemical reaction.
Enzyme speed reactions by lowering EA.

The transition state can then be reached even at moderate temperatures.
Enzymes do not change delta G.

Because enzymes are so selective, they determine which chemical processes will occur at any time.
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Fig. 8-14
Transition state
A C
B D
EA
Reactants
A
C
B
G < O D
Products
The Activation Energy Barrier

Every chemical reaction between molecules involves bond breaking and bond forming The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA) Activation energy is often supplied in the form of heat from the surroundings
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Enzymes catalyze reactions by lowering the EA barrier Enzymes do not affect the change in free energy (G); instead, they hasten reactions that would occur eventually
How Enzymes Lower the EA Barrier
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Course of reaction without enzyme
EA without enzyme
EA with enzyme is lower
Reactants Course of reaction with enzyme G is unaffected by enzyme
Products
2. Enzymes are substrate specific

A substrate is a reactant which binds to an enzyme. When a substrate or substrates binds to an enzyme, the enzyme catalyzes the conversion of the substrate to the product.
Sucrase is an enzyme that binds to sucrose and breaks the disaccharide into fructose and glucose.
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The shape of active site matches the shape of a specific part of the substrate molecule. Induced Fit
Substrate molecule upon binding to the active site of the enzyme induces a slight change in the shape of both molecule, substrate and enzyme. Once substrate molecule has made contact with the active site and has initiated the change in shape, the enzyme initiates the actual reaction of the substrate molecule. Once the reaction complete, attraction between substrate and enzyme cease, freeing the enzymes from the product enabling to catalyzed the second reaction of the same type.
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The active site of an enzymes is a groove on the surface of the protein into which the substrate fits. The specificity of an enzyme is due to the fit between the active site and the substrate. As the substrate binds, the enzyme changes shape leading to a tighter induced fit, bringing chemical groups in position to catalyze the reaction.
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The reason a particular enzyme will combine only with one kind of substrate is that the fit between the two is very precise. In fact, the fit is so precise, the combining of the enzyme and substrate results in a slight change in the shape of both. This precise fit that modifies both original molecules is called an induced fit. This "strained" fit acts to break old chemical bonds and form new ones, resulting in the formation of the product from the substrate. Once this change has occurred, the product is released from the enzyme, and the enzyme can combine with another molecule of substrate.
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In most cases substrates are held in the active site by weak interactions, such as hydrogen bonds and ionic bonds.
3. The active site is an enzymes catalytic center
R groups of amino acids on the active site catalyze the conversion of substrate to product.
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In an enzymatic reaction, the substrate binds to the active site of the enzyme The active site can lower an EA barrier by
Orienting substrates correctly Straining substrate bonds Providing a favorable microenvironment Covalently bonding to the substrate
Catalysis in the Enzymes Active Site
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Enzymes speed up metabolic reactions by lowering energy barriers A catalyst is a chemical agent that speeds up a reaction without being consumed by the reaction An enzyme is a catalytic protein Hydrolysis of sucrose by the enzyme sucrase is an example of an enzymecatalyzed reaction
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Fig. 8-16
Substrate
Active site
Enzyme (a) (b)
Enzyme-substrate complex
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A single enzyme molecule can catalyze thousands or more reactions a second. Enzymes are unaffected by the reaction and are reusable. Most metabolic enzymes can catalyze a reaction in both the forward and reverse direction.
The actual direction depends on the relative concentrations of products and reactants. Enzymes catalyze reactions in the direction of equilibrium.
Enzymes use a variety of mechanisms to lower activation energy and speed a reaction.
As the active site binds the substrate, it may put stress on bonds that must be broken, making it easier to reach the transition state.
R groups at the active site may create a conducive microenvironment for a specific reaction.
The active site orients substrates in the correct orientation for the reaction.
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The rate that a specific number of enzymes converts substrates to products depends in part on substrate concentrations. At low substrate concentrations, an increase in substrate speeds binding to available active sites. However, there is a limit to how fast a reaction can occur. At some substrate concentrations, the active sites on all enzymes are engaged, called enzyme saturation. The only way to increase productivity at this point is to add more enzyme molecules.
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Michaelis-Menten E + S --- k1k2 ES--- k3 E + P

S reacts with E, and turns into ES, with rate constant k1, which turns into P and regenerates E, with rate constant k3. Now, ES can turn back into S and E, with rate constant k2. The Michaelis-Menten mechanism for enzymic catalysis follows this path.
E = free enzymes, S = substrate, ES = enzymessubstrate complex, P = product, e = total enzyme concentration.
K1 = rate constant for formation ES K2 = rate constant for dissociation of ES to E and S. K3 = rate constant for dissociation of ES to E and P Free Powerpoint Templates Page 61
Effect of enzyme concentration on reaction velocity

If the substrate concentration constant, velocity of reaction is proportional to the enzyme concentration. Enzyme concentration is propotional to velocity of reaction Vmax
Reaction velocity (V)

V max
Km
Substrate concentration at V
max
[S]
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ATP + H2O
Energy from catabolism (exergonic, energy-releasing processes)
ADP + P i
Energy for cellular work (endergonic, energy-consuming processes)
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Fig. 8-13
Sucrose (C12H22O11)
Sucrase
Glucose (C6H12O6) Free Powerpoint Templates Fructose (C6H12O6)
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Substrate Specificity of Enzymes

The reactant that an enzyme acts on is called the enzymes substrate The enzyme binds to its substrate, forming an enzyme-substrate complex The active site is the region on the enzyme where the substrate binds Induced fit of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
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Fig. 8-17
1 Substrates enter active site; enzyme

changes shape such that its active site enfolds the substrates (induced fit).
2 Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. 3 Active site can lower EA
Substrates
Enzyme-substrate complex
and speed up a reaction.
6
Active site is available for two new substrate molecules.
Enzyme
Products 5 are released.
4 Substrates are converted to products. Free Powerpoint Templates Products
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An enzymes activity can be affected by

General environmental factors, such as temperature and pH Chemicals that specifically influence the enzyme
Effects of Local Conditions on Enzyme Activity
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Effects of Temperature and pH

Each enzyme has an optimal temperature in which it can function Each enzyme has an optimal pH in which it can function
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Optimal temperature for typical human enzyme

Rate of reaction
Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria
40 60 80 Temperature (C) (a) Optimal temperature for two enzymes

0 20
100
Optimal pH for pepsin (stomach enzyme) Rate of reaction
Optimal pH for trypsin

(intestinal enzyme)
4 5 pH (b) Optimal pH for two enzymes 0 1 2 3
10
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Cofactors
Cofactors are nonprotein enzyme helpers Cofactors may be inorganic (such as a metal in ionic form) or organic An organic cofactor is called a coenzyme Coenzymes include vitamins
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Enzyme Inhibitors
Competitive inhibitors bind to the active site of an enzyme, competing with the substrate Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective Examples of inhibitors include toxins, poisons, pesticides, and antibiotics
Fig. 8-19
Substrate Active site Competitive inhibitor Enzyme
Noncompetitive inhibitor (a) Normal binding (b) Competitive inhibition (c) Noncompetitive inhibition
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inhibitors, prevent enzymes from catalyzing reactions.

If binding involves covalent bonds, then inhibition is often irreversible. If binding is weak, inhibition may be reversible.
If the inhibitor binds to the same site as the substrate, then it blocks substrate binding via competitive inhibition.
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If the inhibitor binds somewhere other than the active site, it blocks substrate binding via noncompetitive inhibition. Binding by the inhibitor causes the enzyme to change shape, rendering the active site unreceptive or less effective at catalyzing the reaction. Reversible inhibition of enzymes is a natural part of the regulation of metabolism.
Reversible inhibitor: A substance that forms a weak bonds with an enzyme, temporarily interfering with its function. A reversible inhibitor can be competitive or non competitive. Irreversible inhibitor: A substance that permanently inactivates an enzyme.
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Competitive inhibition reversible

Example: succinate dehydrogenase inhibit by malonate and oxaloacetate. It is activated by ATP, Pi and succinate.
Succinate + FAD -- Fumarate + FADH2
Irreversible inhibitors: These molecules bind permanently with the enzyme molecule and so effectively reduce the enzyme concentration, thus limiting the rate of reaction, for example, cyanide irreversibly inhibits the enzyme cytochrome oxidase found in the electron transport chain used in respiration. If this enzyme cannot be used, death will occur.
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Chemical chaos would result if a cells metabolic pathways were not tightly regulated A cell does this by switching on or off the genes that encode specific enzymes or by regulating the activity of enzymes
Regulation of enzyme activity helps control metabolism

Allosteric Regulation of Enzymes

Allosteric regulation may either inhibit or stimulate an enzymes activity Allosteric regulation occurs when a regulatory molecule binds to a protein at one site and affects the proteins function at another site
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Allosteric Activation and Inhibition

Most allosterically regulated enzymes are made from polypeptide subunits Each enzyme has active and inactive forms The binding of an activator stabilizes the active form of the enzyme The binding of an inhibitor stabilizes the inactive form of the enzyme
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Fig. 8-20
Allosteric enyzme Active site with four subunits (one of four)
Regulatory site (one of four)
Activator
Active form
Stabilized active form
Oscillation
NonInhibitor functional Inactive form active site
Stabilized inactive form
(a) Allosteric activators and inhibitors Substrate
Inactive form
(b) Cooperativity: another type of allosteric activation
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Fig. 8-20a
Allosteric enzyme with four subunits
Active site (one of four)
Regulatory site (one of four)
Activator Active form Stabilized active form
Oscillation
NonInhibitor Inactive form functional active site
Stabilized inactive form
(a) Allosteric activators and inhibitors Free Powerpoint Templates
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Cooperativity is a form of allosteric regulation that can amplify enzyme activity In cooperativity, binding by a substrate to one active site stabilizes favorable conformational changes at all other subunits
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Fig. 8-20b
Substrate
Inactive form
(b) Cooperativity: another type of allosteric activation
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In enzymes with multiple catalytic subunits, binding by a substrate to one active site stabilizes favorable conformational changes at all other subunits, a process called cooperativity. This mechanism amplifies the response of enzymes to substrates, priming the enzyme to accept additional substrates
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Identification of Allosteric Regulators

Allosteric regulators are attractive drug candidates for enzyme regulation
Page 84
Some allosteric regulators, activators, stabilize the conformation that has a functional active site. Other regulators, inhibitors, stabilize the conformation that lacks an active site.
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Metabolic control often depends on allosteric regulation In many cases, the molecules that naturally regulate enzyme activity behave like reversible noncompetitive inhibitors. These molecules often bind weakly to a allosteric site, a specific receptor on the enzyme that is not the active site. Binding by these molecules can either inhibit or stimulate enzyme activity.
Most allosterically regulated enzymes are constructed of two or more polypeptide chains. Each subunit has its own active site and allosteric sites are often located where subunits join. The whole protein oscillates between two conformational shapes, one active, one inactive.
Page 87
As the chemical conditions in the cell shift, the pattern of allosteric regulation will shift as well. In many cases both inhibitors and activators are similar enough in shape that they compete for the same allosteric sites.
These molecules may be products and substrates of a metabolic pathway. For example, some catabolic pathways have allosteric sites that are inhibited when ATP binds and activated when AMP binds. When ATP levels are low, AMP levels are high, and the pathway is turned on until ATP Free levels Powerpoint Templates Page 88 levels rise, AMP fall and inhibition by
Fig. 8-21
EXPERIMENT Caspase 1 Active site Substrate
SH Known active form
SH Active form can bind substrate
SH Allosteric binding site Allosteric Known inactive form inhibitor
SS Hypothesis: allosteric inhibitor locks enzyme in inactive form
RESULTS Caspase 1
Active form
Free
Inhibitor Allosterically Inactive form inhibited form Powerpoint Templates
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Fig. 8-21a
EXPERIMENT
Caspase 1 Active site Substrate
SH Known active form
SH Active form can bind substrate
binding site Allosteric Known inactive form inhibitor
SH Allosteric
SS
Hypothesis: allosteric inhibitor locks enzyme in inactive form Free Powerpoint Templates Page 90
Fig. 8-21b
RESULTS
Caspase 1
Inhibitor Active form Allosterically inhibited form
Inactive form
Page 91
Structures within the cell help bring order to metabolic pathways Some enzymes act as structural components of membranes In eukaryotic cells, some enzymes reside in specific organelles; for example, enzymes for cellular respiration are located in mitochondria
Specific Localization of Enzymes Within the Cell
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Fig. 8-23
Mitochondria
1 m
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Course of reaction without enzyme
EA without enzyme
EA with enzyme is lower
Reactants Course of reaction with enzyme G is unaffected by enzyme
Products Progress of the reaction

A cells physical and chemical environment affects enzyme activity The three-dimensional structures of enzymes (almost all proteins) depend on environmental conditions. Changes in shape influence the reaction rate. Some conditions lead to the most active conformation and lead to optimal rate of reaction.
1. Temperature has a major impact on reaction rate.

As temperature increases, collisions between substrates and active sites occur more frequently as molecules move faster. However, at some point thermal agitation begins to disrupt the weak bonds that stabilize the proteins active conformation and the protein denatures. Each enzyme has an optimal temperature.
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2. Because pH also influences shape and therefore reaction rate, each enzyme has an optimal pH too. This falls between pH 6 - 8 for most enzymes. However, digestive enzymes in the stomach are designed to work best at pH 2 while those in the intestine are optimal at pH 8, both matching their working environments.
Fig. 8-UN4
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3. Amount of enzyme present

The amount of enzyme present is determined by its rate of synthesis (ks) and the rate of degradation (kd). Enzyme turnover.
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Many enzymes require nonprotein helpers, cofactors, for catalytic activity.

They bind permanently to the enzyme or reversibly. Some inorganic cofactors include zinc, iron, and copper.
Organic cofactors, coenzymes, include vitamins or molecules derived from vitamins.
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Feedback Inhibition
In feedback inhibition, the end product of a metabolic pathway shuts down the pathway Feedback inhibition prevents a cell from wasting chemical resources by synthesizing more product than is needed
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One of the common methods of metabolic control is feedback inhibition metabolic pathway is turned off by its end product. The end product acts as an inhibitor of an enzyme in the pathway. When the product is abundant the pathway is turned off, when rare the pathway is active.
Systematic names for each enzyme have been made in an international claasification of enzymes.
Oxidoreductase: are involved in oxidation/reduction. Transferase: transfer functional groups between donor and receptor. Hydrolases transfer water that is they catalysed the hydrolysis of a substrate. Lyases: add or remove the element of water, ammonia or CO2 to form double bond. Isomerase: catalyzed changes within one molecule. Ligase (synthetases): join two molecule together at the expense of a high-energy phosphate bond of ATP.
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ENZYMES

Free Powerpoint Templates

Overview: The Energy of Life

Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Free Powerpoint Templates

Organization of the Chemistry of Life into Metabolic Pathways

Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Free Powerpoint Templates

Free Powerpoint Templates

Free Powerpoint Templates

Free Powerpoint Templates

Free Powerpoint Templates

Chemical energy is potential energy available for release in a chemical reaction

Diving converts potential energy to kinetic energy.

Climbing up converts the kinetic energy of muscle movement to potential energy.

The Laws of Energy Transformation

The First Law of Thermodynamics

The first law is also called the principle of conservation of energy

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The Second Law of Thermodynamics

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(a) First law of thermodynamics

(b) Second law of thermodynamics

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Biological Order and Disorder

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Free Powerpoint Templates

Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Free Energy and Metabolism

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Exergonic and Endergonic Reactions in Metabolism

Free Powerpoint Templates

Fig. 8-6 Reactants Free energy Amount of energy released (G < 0)

Progress of the reaction (a) Exergonic reaction: energy released

Amount of energy required (G > 0)

Progress of the reaction

(b) Endergonic reaction: energy required

Equilibrium and Metabolism

A defining feature of life is that metabolism is never at equilibrium

Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Free Powerpoint Templates

ATP powers cellular work by coupling exergonic reactions to endergonic reactions

The Structure and Hydrolysis of ATP

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Phosphate groups Ribose

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Adenosine triphosphate (ATP)

Adenosine diphosphate (ADP)

How ATP Performs Work

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(a) Transport work: ATP phosphorylates transport proteins ATP

The Regeneration of ATP

Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

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Energy from catabolism (exergonic, energy-releasing processes)

Energy for cellular work (endergonic, energy-consuming processes)

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1. Enzymes speed up metabolic reactions by lowering energy barriers

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