Metabolism and Energy. Mrs. Stahl AP Biology
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1 Metabolism and Energy Mrs. Stahl AP Biology
2 The Energy of Life The living cell is a miniature chemical factory where thousands of reactions occur The cell extracts energy stored in sugars and other fuels and applies energy to perform work Some organisms even convert energy to lightbioluminescence
3 Figure 8.1
4 Forms of Energy Energy is the capacity to cause change Energy exists in various forms, some of which can perform work
5 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
6 A diver has more potential energy on the platform than in the water. Figure 8.2 Diving converts potential energy to kinetic energy. Climbing up converts the kinetic energy of muscle movement to potential energy. A diver has less potential energy in the water than on the platform.
7 The Laws of Energy Transformation Thermodynamics is the study of energy transformations An isolated system, such as that approximated by liquid in a thermos, is unable to exchange energy or matter with its surroundings In an open system, energy and matter can be transferred between the system and its surroundings Organisms are open systems
8 The First Law of Thermodynamics 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 is also called the principle of conservation of energy
9 Plants do not produce energy, they transform light energy to chemical energy. During every transfer, some energy is converted to heat -> a system can use heat to do work only when there is a difference that results in heat flowing from warmer locations to cooler ones. If heat is uniform as in a living cell, heat can only be used to warm the organism.
10 Figure 8.3 Heat CO 2 Chemical energy H 2 O (a) First law of thermodynamics (b) Second law of thermodynamics
11 The Second Law of Thermodynamics 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 Entropy- measure of disorder or randomness Increase entropy = increase heat
12 Living cells unavoidably convert organized forms of energy to heat Spontaneous processes occur without energy input; they can happen quickly or slowly. Living systems create ordered structures from less ordered starting materials. Ex- amino acids are ordered into polypeptide chains Ex- structure of a multicellular body is organized and complex. For a process to occur without energy input, it must increase the entropy of the universe
13 Highly Ordered Living Organisms Do Not Violate the Second Law of Thermodynamics Organisms also take in organized forms of matter and energy from its surrounding and replaces them with less ordered forms. Ex- animal consumes organic molecules as food and catabolizes (breaks down -> metabolism) them to low energy molecules such as carbon dioxide and water.
14 The evolution of more complex organisms does not violate the second law of thermodynamics because Earth and organisms are open systems. We get our energy from the sun and we can evolve and create order by increasing the disorder of the universe. Entropy (disorder) may decrease in an organism, but the universe s total entropy increases
15 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.
16 Free-Energy Change, G A living system s free energy is energy that can do work when temperature and pressure are uniform, as in a living cell
17 The change in free energy ( G) during a process is related to the change in enthalpy, or change in total energy ( H), change in entropy ( S), and temperature in Kelvin units (T) G = H - T S H= enthalpy, in a spontaneous reaction it gets smaller or decreases because energy is released. S= entropy, measure of the disorder. In a spontaneous reaction entropy increases. T= temperature, when temperature increases the spontaneous reaction is more likely to happen. What makes G decrease? A decrease in H An increase in S An increase in T Only processes with a negative G are spontaneous also known as exergonic ( releases free energy as heat)
18 G > 0 = endergonic reaction, energy must be added G = 0 = equilibrium Increases in temperature amplify the entropy. Think about a cherry bomb-> add heat and it blows up. Not all the energy in a system is available for work because the entropy component must be subtracted from the enthalpy component. What remains is the free energy, referred to as the stability of the system.
19 Figure 8.5b (a) Gravitational motion (b) Diffusion (c) Chemical reaction
20 Exergonic and Endergonic Reactions in Exergonic Reaction: Metabolism G is negative, Spontaneous The products of the reaction contain less free energy than reactants. Bond is lower or disorder is higher or both. Energy is released. Ex- Cellular Respiration Endergonic reaction: absorbs free energy from its surroundings and is non-spontaneous Energy must be supplied, ex- photosynthesis
21 Free energy Free energy (a) Exergonic reaction: energy released, spontaneous Reactants Energy Products Amount of energy released ( G < 0) (b) Progress of the reaction Endergonic reaction: energy required, nonspontaneous Products Reactants Energy Amount of energy required ( G > 0) Progress of the reaction
22 If all chemical reactions that release free energy tend to occur spontaneously, why haven t all such reactions already occurred? Most reactions require an input of energy to get started such as endergonic reactions (photosynthesis).
23 Activation Energy Before any bonds can form, they have to be broken by energy input. Defined as the extra energy needed to destabilize existing chemical bonds and initiate / start a chemical reaction. Exergonic rate depends on the activation energy required for the reaction to begin. Rates of reactions are increased by: Increasing the energy of reacting molecules Lowering activation energy
24 Catalysis / Catalysts A substance that lowers the activation energy Ex- enzymes They cannot make an endergonic reaction proceed spontaneously.
25 Adenosine Triphosphate- ATP Main energy currency in all living cells 1. Makes sugars 2. Supplying activation energy for chemical reactions 3. Actively transporting substances across membranes 4. Moving through the environment and growing
26 The Structure and Hydrolysis of ATP ATP (adenosine triphosphate) is the cell s energy shuttle ATP is composed of ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups
27 How does ATP store energy? The energy is stored in the bonds between the triphosphates. These groups repel each other due to their negative charges, and the covalent bonds joining the phosphates are unstable and can break. They are easily broken by hydrolysis and when they break they release and transfer a large amount of energy which can be used.
28 Figure 8.9a Adenine Triphosphate group (3 phosphate groups) Ribose (a) The structure of ATP
29 Figure 8.9b Adenosine triphosphate (ATP) H 2 O Energy Inorganic phosphate Adenosine diphosphate (ADP) (b) The hydrolysis of ATP
30 How does ATP become ADP? The bonds are broken on the third phosphate, releasing energy. ATP -> ADP +Pi Energy = 7.3kcal / mol This release of energy comes from the chemical change to a state of lower free energy, not from the phosphate bonds themselves
31 Why does the hydrolysis of ATP yield so much energy? The release of energy initially comes from the chemical change to a state of lower free energy. Each phosphate group has a negative charge. Three like charges are crowded together and their mutual repulsion contributes to the instability of the molecule.
32 How the Hydrolysis of 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
33 ATP drives endergonic reactions by phosphorylation, transferring a phosphate group to some other molecule, such as a reactant The recipient molecule is now called a phosphorylated intermediate
34 Transport and mechanical work in the cell are also powered by ATP hydrolysis ATP hydrolysis leads to a change in protein shape and binding ability
35 Transport protein Solute Figure 8.11 ATP ADP P i P P i Solute transported (a) Transport work: ATP phosphorylates transport proteins. Vesicle Cytoskeletal track ATP ATP ADP P i (b) Motor protein Protein and vesicle moved Mechanical work: ATP binds noncovalently to motor proteins and then is hydrolyzed.
36 What reactions does ATP Drive? Endergonic Reactions
37 Figure 8.12 ATP H 2 O Energy from catabolism (exergonic, energyreleasing processes) ADP P i Energy for cellular work (endergonic energy-consuming processes)
38 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 ATP cycle is a revolving door through which energy passes during its transfer from catabolic to anabolic pathways
39 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 Substrate- The molecules that will undergo the reaction An enzyme is a catalytic protein Hydrolysis of sucrose by the enzyme sucrase is an example of an enzyme-catalyzed reaction
40 Figure 8.UN02 Sucrase Sucrose (C 12 H 22 O 11 ) Glucose (C 6 H 12 O 6 ) Fructose (C 6 H 12 O 6 )
41 Functions of Enzymes 1. Lowers the activation energy required for new bonds to form 2. Speeds up the rate of reaction 3. Regulates metabolic pathways
42 What is the importance of carbonic acid in vertebrate red blood cells? Vertebrate RBC s have an enzyme called carbonic anhydrase, which aids in breaking down carbon dioxide in our blood. 600,000 molecules of carbonic acid form every second. This enzyme increases the rate of reaction one million times.
43 The Active Site They are pockets on the enzyme where the substrates fit perfectly.
44 Catalysis in the Enzyme s Active Site In an enzymatic reaction, the substrate binds to the active site of the enzyme The active site can lower an E A barrier by Orienting substrates correctly Straining substrate bonds Providing a favorable microenvironment Covalently bonding to the substrate
45 Enzyme Substrate Complex A substrate molecule binds with an enzyme at its active site. Chemical reactions occur and bonds are either broken or new ones are formed. The substrates have been changed into products. The products leave the enzyme and the process starts all over again.
46 Induced Fit When the active site changes its shape slightly so that it can bind onto the substrate more tightly.
47 Figure 8.15 Substrate Active site Enzyme Enzyme-substrate complex
48 Where are most enzymes found? Cytoplasm Cell membranes Organelles
49 Multienzyme Complexes and Advantages They allow a plethora of chemical reactions to occur-> molecular machine Advantages: 1. All reactions can be controlled as a unit 2. No unwanted side reactions 3. Rate of the enzyme is limited
50 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 (E A ) Activation energy is often supplied in the form of thermal energy that the reactant molecules absorb from their surroundings
51 Free energy Figure A B 8.13 C D Transition state A C B D E A Reactants A C B D G < O Products Progress of the reaction
52 Animation: How Enzymes Work
53 1 Substrates enter 2 active site. Figure Substrates are held in active site by weak interactions. Substrates Enzyme-substrate complex
54 1 Substrates enter 2 active site. Figure Substrates are held in active site by weak interactions. Substrates Enzyme-substrate complex 3 Substrates are converted to products.
55 1 Substrates enter 2 active site. Figure Substrates are held in active site by weak interactions. Substrates Enzyme-substrate complex 4 Products are released. Products 3 Substrates are converted to products.
56 1 Substrates enter 2 active site. Figure Substrates are held in active site by weak interactions. Substrates Enzyme-substrate complex 5 Active site is available for new substrates. Enzyme 4 Products are released. Products 3 Substrates are converted to products.
57 Effects of Local Conditions on Enzyme Activity An enzyme s activity can be affected by General environmental factors, such as temperature and ph Chemicals that specifically influence the enzyme
58 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 Optimal conditions favor the most active shape for the enzyme molecule
59 Temperature Above the optimal temperature= forces are too weak to maintain the enzymes shape -> denatures Below optimum temperatures= hydrogen bonds and hydrophobic interactions that determine the enzymes shape is not flexible to allow induced fit. Humans= 35 to 40 Celcius Prokaryotes= 70 Celcius (hot springs)
60 ph Interactions are sensitive to the hydrogen ion concentration of the fluid in which the enzyme is dissolved, changing the concentration. Shifts the balance between +/- amino acids Optimum ph= 6 to 8
61 Rate of reaction Rate of reaction Optimal temperature for typical human enzyme (37 C) Figure 8.17 Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria (77 C) Temperature ( C) (a) Optimal temperature for two enzymes Optimal ph for pepsin (stomach enzyme) Optimal ph for trypsin (intestinal enzyme) ph (b) Optimal ph for two enzymes
62 Enzyme Inhibitors- substance that binds to an enzyme and decreases its activity 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. Binds at the allosteric site. Examples of inhibitors include toxins, poisons, pesticides, and antibiotics
63 Figure 8.18 (a) Normal binding (b) Competitive inhibition (c) Noncompetitive inhibition Substrate Active site Enzyme Competitive inhibitor Noncompetitive inhibitor
64 Allosteric enzymes- enzymes that exist as either active or inactive Allosteric site- on /off chemical switches Allosteric inhibitors- binds to the allosteric site and reduces enzyme activity Allosteric Activator- keeps the enzyme active, increases enzyme activity
65 Cofactors Cofactors are non-protein enzyme helpers that are found around the active site to assist in catalysis. They help weaken bonds and make them easier to break. Cofactors may be inorganic (such as a metal in ionic form) or organic An organic cofactor is called a coenzyme Coenzymes serve as an electron acceptor which then transfers the electrons to a different enzyme, which releases them to the substrates in another reaction (Ex- NADP)
66 The Evolution of Enzymes Enzymes are proteins encoded by genes Changes (mutations) in genes lead to changes in amino acid composition of an enzyme Altered amino acids in enzymes may result in novel enzyme activity or altered substrate specificity Under new environmental conditions a novel form of an enzyme might be favored For example, six amino acid changes improved substrate binding and breakdown in E. coli
67 Regulation of enzyme activity helps control metabolism Chemical chaos would result if a cell s 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
68 Localization of Enzymes Within the Cell 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
69 Metabolism Totality of an organism s chemical reaction. Emergent property of life that arises from interactions between molecules within the orderly environment of the cell.
70 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
71 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 energy flows through living organisms
72 Biochemical Pathways Organizational units of metabolism. The elements an organism needs / controls to achieve metabolic activity. They think they came from early oceans, creating an organic soup.
73 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
74 Cells! 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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