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1 Module 2D - Energy and Metabolism Objective # 19 All living organisms require energy for survival. In this module we will examine some general principles about chemical reactions and energy usage within cells. Define the term energy and distinguish between potential and kinetic energy. 1 2 Objective 19 Energy is the ability to cause change. Any change in the universe requires energy. Energy comes in 2 forms: Potential energy is stored energy. No change is currently taking place Kinetic energy is currently causing change. This always involves some type of motion. Potential energy Objective 19 Two Forms of Energy Kinetic energy 3 4 Objective # 20 State the first and second laws of thermodynamics and explain how they apply to living i organisms. Thermodynamics is the study of energy changes. Two fundamental laws govern all energy changes in the universe. These 2 laws are simply called the first and second laws of thermodynamics: 5 6 1

2 First Law: Energy can be converted from one form to another, but it cannot be created or destroyed. The total amount of energy in a closed system remains constant. Second Law: Whenever an energy conversion takes place, some of the energy gets converted into a more dispersed and less useful form (usually random molecular motion = heat). 7 8 Free energy (G) is a measure of the amount of energy available to do useful work. It depends on: the total amount of energy present; this is called enthalpy (H) the amount of energy being used for non-useful work (random molecular motion); this is called entropy (S). 9 In general, ΔG G = ΔH -T ΔS, where T represents the temperature in degrees Kelvin and Δ represent the change in. This means the amount of energy available for useful work (G) equals the total energy present (H) minus the energy that is being wasted on random molecular motion (S). 10 In summary, whenever an energy change takes place in a closed system, the first law tells us the total energy remains constant the h second law tells us free energy decreases. How is this possible? entropy increases! So closed systems tend to become more disorganized. 11 Objective # 21 Explain what a chemical reaction is and discuss how chemical equations are used to describe the changes that take place during a chemical reaction. 12 2

3 Objective 21 Most of the changes that take place in living organisms are the result of chemical reactions. What is a chemical reaction? As atoms and molecules move around, they collide with each other. If they collide with enough force, existing chemical bonds can break and new bonds can form. 13 Objective 21 Chemical equations can be used to describe the changes that take place during a chemical reaction: CH 4 + 2O 2 CO 2 + 2H 2 O Reactants Products During a chemical reaction no atoms are created or destroyed. 14 Objective 21 Most reactions are reversible: reading from left to right is called the forward reaction reading g from right to left is called the reverse reaction At equilibrium, the rate of the forward reaction equals the rate of the reverse reaction. 15 Objective # 22 Distinguish between endergonic and exergonic reactions and explain how they are coupled in living organisms. Describe the roles of ATP and ADP in the coupling of chemical reactions. 16 Objective 22 Chemical reactions involve a change in free energy as well as a change in the types of molecules present. 17 Objective 22 All atoms and molecules have a certain amount of free energy: potential energy stored in the chemical bonds that hold them together. kinetic energy due to their constant random motion. Large, complex molecules have more free energy than small molecules. 18 3

4 Objective 22 Exergonic reactions: the reactants have more free energy than the products: C 6 H 12 O 6 + 6O 2 6CO 2 + 6H 2 O more free energy less free energy involve a net release of energy and/or an increase in entropy occur spontaneously (without a net input of energy) 19 Objective 22 Endergonic reactions: the reactants have less free energy than the products: 6CO 2 + 6H 2 O C 6H 12 O 6 + 6O 2 less free energy more free energy involve a net input of energy and/or a decrease in entropy do not occur spontaneously 20 Exergonic and Endergonic Reactions Energy supplied Energy released Reactant Endergonic Product Energy must be supplied. Reactant Exergonic Energy is released. Product 21 Objective 22 Living organisms have the ability to couple exergonic and endergonic reactions: energy g released by exergonic reactions is captured and used to make ATP from ADP and Pi ATP can be broken back down to ADP and Pi, releasing energy to power the cell s endergonic reactions. 22 ATP Adenosine triphosphate The energy currency for all cells Composed of Ribose 5 carbon sugar Adenine Chain of 3 phosphates Key to energy storage Bonds are unstable ADP 2 phosphates AMP 1 phosphate lowest energy form 23 Structure of ATP 24 4

5 The ATP Cycle Objective # 23 Explain the concepts of chemical equilibrium, transition state, and activation i energy Objective 23 All reactions, both endergonic and exergonic, require an input of energy to get started. This energy is called activation energy. Activation i energy is needed d to bring the reactants close together and weaken existing bonds. This produces an unstable state of maximum potential energy called the transition state. 27 Energy supplied Energy released Transition State Reactant Product Activation energy 28 Objective # 24 Describe some methods that can be used to speed up chemical reactions. Objective 24 In most cases, molecules do not have enough kinetic energy to reach the transition state when they collide. Therefore, most collisions are non- productive, and the reaction proceeds very slowly if at all. What can be done to speed up these reactions?

6 Objective 24 1) Add Heat molecules move faster so they collide more frequently and with greater force. 2) Add a catalyst a catalyst reduces the energy needed to reach the activation state, without being changed itself. Proteins that function as catalysts are called enzymes. Energy supplied Energy released Activation Energy and Catalysis Reactant Product Uncatalyzed Activation energy Reactant Catalyzed Activation energy Product Objective 24 Unlike heat, which speeds up all reactions indiscriminately, enzymes are highly specific. Each enzyme typically speeds up only one or a few similar chemical reactions. Therefore, by controlling which enzymes are made, a cell can control which reactions take place in the cell. Objective # 25 Describe the structure, function, and characteristics of enzymes Objective 25 Almost all enzymes are globular proteins with one or more pockets on their surface called active sites. Reactants bind to the active site to form an enzyme-substrate complex. The 3-D shape of the active site and the substrates must match, like a lock and key. Objective 25 Binding of the substrates causes the enzyme to adjust its shape slightly, leading to a better induced fit. When this happens, the substrates are brought close together and existing bonds are stressed. This reduces the amount of energy needed to reach the transition state

7 Binding of the substrates causes the enzyme to adjust its shape slightly, leading to a better induced fit Objective # 26 Explain how the following factors can affect enzyme activity: a) temperature b) ph c) inhibitors and activators d) cofactors Objective 26 The rate of an enzyme-catalyzed reaction is affected by the concentration of both the enzyme and its substrates. In addition, any physical or chemical factors that affect the enzyme s 3-D shape can affect the enzyme s ability to catalyze the reaction Objective 26a & b Temperature and ph: Most enzymes have an optimum temperature and an optimum ph. These are related to the environment where the enzyme normally functions. Enzyme activity decreases above or below the optimum

8 Relationship of Enzyme Activity to Temperature Relationship of Enzyme Activity to ph Rate of Reaction Optimum temperature for human enzyme Optimum temperature for enzyme from hotsprings prokaryote Temperature of Reaction ( o C) eaction Rate of Re Optimum ph for pepsin Optimum ph for trypsin ph of Reaction Objective 26c Inhibitors and activators are substances that bind to an enzyme and affect its ability to catalyze a reaction. Activators bind to a region of the enzyme called the allosteric site, thereby maintaining the enzyme s active configuration and its activity. 45 Objective 26c Inhibitors decrease enzyme activity in one of 2 ways: 1)competitive inhibitors bind to the active site, thereby preventing the substrates from binding. 2)noncompetitive inhibitors bind to an allosteric site, thereby altering the shape of the active site so that it cannot bind to the substrate. 46 Substrate Substrate Active site Inhibitor Active site Inhibitor Enzyme Enzyme Allosteric site When an inhibitor joins to an allosteric site and alters the shape of the active site so it cannot bind to the substrate, this is called Noncompetitive inhibition 47 When an inhibitor binds to the active site of an enzyme and blocks the substrate from binding, this is called Competitive inhibition 48 8

9 Objective 26d Cofactors are nonprotein substances required by enzymes in order to function. For example, the active site of many enzymes contain metal ions that help draw electrons away from the substrates. Organic molecules that function as cofactors are called coenzymes. Objective # 27 Define the terms metabolism and metabolic pathway (or biochemical i pathway ) and explain how metabolic pathways are regulated Objective 27 Metabolism refers to the sum of all chemical reactions carried out by an organism: reactions that join small molecules together to form larger, more complex molecules are called anabolic. reactions that break large molecules down into smaller subunits are called catabolic. 51 Objective 27 A sequence of chemical reactions, where the product of one reaction serves as a substrate for the next, is called a metabolic pathway (or biochemical pathway). Most metabolic pathways take place in specific regions of the cell Objective 27 The regulation of simple metabolic pathways often depends on feedback inhibition: the end product of the pathway binds to an allosteric site on the enzyme that catalyzes the first reaction and inactivates it. Why is the first reaction targeted? 54 9

10 55 10

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