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Chapter 8 Pictures

Chapter 8 Pictures. Potential and Kinetic Energy. 2 nd Law of Thermodynamics. Kinetic Energy 25% drives the pistons 75% lost as heat. Potential Energy-Fuel. *In every chemical reaction, some energy is lost as heat. Enzyme 1. Enzyme 2. Enzyme 3. A. D. C. B. Reaction 1. Reaction 2.

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Chapter 8 Pictures

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  1. Chapter 8 Pictures

  2. Potential and Kinetic Energy

  3. 2nd Law of Thermodynamics Kinetic Energy 25% drives the pistons 75% lost as heat Potential Energy-Fuel *In every chemical reaction, some energy is lost as heat.

  4. Enzyme 1 Enzyme 2 Enzyme 3 A D C B Reaction 1 Reaction 2 Reaction 3 Startingmolecule Product Theoretical metabolic pathway

  5. Fig 5.2. Catabolic vs. Anabolic Reactions • Condensation → reactions (anabolic) • Hydrolysis →reactions (catabolic)

  6. Catabolic Rxns – • O-O O + O + Energy • Anabolic Rxns- O + O + Energy O-O Figure 8.6

  7. Fig 8.14 Energy Profile for a Catabolic (Exergonic) Reaction ALL rxns require some input of energy In exergonic rxns ∆G is a negative number

  8. Question 8.1 fructose + glucose + H2O Example 2: Sucrose hydrolysis (very slow reaction) Example 1: Baking soda + vinegar (fast reaction)

  9. Examples of an exergonic and endergonic reaction + Ammonia Glutamic Acid Glutamine ΔG = - 3.4 kcal/mol + Ammonia Glutamic Acid Glutamine ΔG = + 3.4 kcal/mol

  10. Chemical Equilibrium

  11. An organism in metabolic equilibrium

  12. Equilibrium ATP

  13. Metabolic Disequilibrium Food ATP ATP ATP Waste Products

  14. Fig 8.3

  15. Chapter 8-ATP

  16. ATP = Currency of the Cell

  17. Fig 8.11

  18. Fig 8.9 ATP hydrolysis

  19. Fig 8.8

  20. Coupled Reactions

  21. Fig 8.10 ATP hydrolysis ATP synthesis

  22. Question 8.2

  23. Chapter 8 - Enzymes

  24. Fig 8.13. Enzyme-catalyzed reaction: hydrolysis by sucrase

  25. Metabolic Map

  26. Fig 8.13. Enzyme-catalyzed reaction: hydrolysis by Sucrase

  27. Fig 8.14Energy Profile Energy (heat) absorbed from the surroundings Energy (heat) released by the reaction

  28. Course of reaction without enzyme EA Fig 8.15 Energy Profile +/- Enzyme without enzyme EA with enzyme is lower Reactants Free energy ∆G is unaffected by enzyme Course of reaction with enzyme Products Progress of the reaction

  29. Fig 8.17

  30. Fig 8.16

  31. Fig 8.18a Optimal temperature for typical human enzyme Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria Rate of reaction 80 0 20 100 40 Temperature (Cº) (a) Optimal temperature for two enzymes

  32. Fig 8.18b Optimal pH for pepsin (stomach enzyme) Optimal pH for trypsin (intestinal enzyme) Rate of reaction 5 6 7 8 9 3 4 0 2 1 (b) Optimal pH for two enzymes

  33. Question 8.3

  34. A substrate can bind normally to the active site of an enzyme. Substrate Active site Enzyme (a) Normal binding A competitive inhibitor mimics the substrate, competing for the active site. Competitive inhibitor Figure 8.19 (b) Competitive inhibition Fig 8.19 a, b

  35. A noncompetitive inhibitor binds to the enzyme away from the active site, altering the conformation of the enzyme so that its active site no longer functions. Noncompetitive inhibitor (c) Noncompetitive inhibition Figure 8.19 Fig 8.19c

  36. Fig 8.21

  37. Question 8.4

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