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Chapter 6: Energy, Enzymes, and Metabolism CHAPTER 6 Energy, Enzymes, and Metabolism.

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Presentation on theme: "Chapter 6: Energy, Enzymes, and Metabolism CHAPTER 6 Energy, Enzymes, and Metabolism."— Presentation transcript:

1 Chapter 6: Energy, Enzymes, and Metabolism CHAPTER 6 Energy, Enzymes, and Metabolism

2 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Energy and Energy Conversions ATP: Transferring Energy in Cells ATP: Transferring Energy in Cells Enzymes: Biological Catalysts Enzymes: Biological Catalysts

3 Chapter 6: Energy, Enzymes, and Metabolism Molecular Structure Determines Enzyme Function Molecular Structure Determines Enzyme Function Metabolism and the Regulation of Enzymes Metabolism and the Regulation of Enzymes

4 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Energy is the capacity to do work.Energy is the capacity to do work. Potential energy is the energy of state or position; it includes energy stored in chemical bonds.Potential energy is the energy of state or position; it includes energy stored in chemical bonds. Kinetic energy is the energy of motion.Kinetic energy is the energy of motion.4

5 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Potential energy can be converted to kinetic energy, which does work. Review Figure 6.16.15

6 Chapter 6: Energy, Enzymes, and Metabolism 6.1 Figure 6.1 figure 06-01.jpg

7 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions The first law of thermodynamics tells us energy cannot be created or destroyed. The second tells us that, in a closed system, the quantity of energy available to do work decreases and unusable energy increases. Review Figure 6.36.37

8 Chapter 6: Energy, Enzymes, and Metabolism 6.3 Figure 6.3 figure 06-03.jpg

9 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Living things obey the laws of thermodynamics. Organisms are open systems that are part of a larger closed system. Review Figure 6.46.49

10 Chapter 6: Energy, Enzymes, and Metabolism 6.4 Figure 6.4 figure 06-04.jpg

11 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Changes in free energy, total energy, temperature, and entropy are related by the equation  G =  H – T  S.Changes in free energy, total energy, temperature, and entropy are related by the equation  G =  H – T  S.11

12 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions Spontaneous, exergonic reactions release free energy and have a negative  G. Non-spontaneous, endergonic reactions take up free energy, have a positive  G, and proceed only if free energy is provided. Review Figure 6.56.512

13 Chapter 6: Energy, Enzymes, and Metabolism 6.5 Figure 6.5 figure 06-05.jpg

14 Chapter 6: Energy, Enzymes, and Metabolism Energy and Energy Conversions The change in free energy of a reaction determines its point of chemical equilibrium, at which forward and reverse reactions proceed at the same rate. For spontaneous, exergonic reactions, the equilibrium point lies toward completion. Review Figure 6.66.614

15 Chapter 6: Energy, Enzymes, and Metabolism 6.6 Figure 6.6 figure 06-06.jpg

16 Chapter 6: Energy, Enzymes, and Metabolism ATP: Transferring Energy in Cells ATP serves as an energy currency in cells.ATP serves as an energy currency in cells. Hydrolysis of ATP releases a relatively large amount of free energy.Hydrolysis of ATP releases a relatively large amount of free energy. Review Figure 6.8 6.8 16

17 Chapter 6: Energy, Enzymes, and Metabolism 6.8 Figure 6.8 figure 06-08.jpg

18 Chapter 6: Energy, Enzymes, and Metabolism ATP: Transferring Energy in Cells The ATP cycle couples exergonic and endergonic reactions, transferring free energy from the exergonic to the endergonic reaction. Review Figures 6.9, 6.106.96.1018

19 Chapter 6: Energy, Enzymes, and Metabolism 6.9 Figure 6.9 figure 06-09.jpg

20 Chapter 6: Energy, Enzymes, and Metabolism 6.10 Figure 6.10 figure 06-10.jpg

21 Chapter 6: Energy, Enzymes, and Metabolism Enzymes: Biological Catalysts The rate of a chemical reaction is independent of  G but is determined by the size of the activation energy barrier.The rate of a chemical reaction is independent of  G but is determined by the size of the activation energy barrier. Catalysts speed reactions by lowering the barrier.Catalysts speed reactions by lowering the barrier. Review Figures 6.11, 6.12 6.116.126.116.1221

22 Chapter 6: Energy, Enzymes, and Metabolism 6.11 Figure 6.11 figure 06-11.jpg

23 Chapter 6: Energy, Enzymes, and Metabolism 6.12 Figure 6.12 figure 06-12.jpg

24 Chapter 6: Energy, Enzymes, and Metabolism Enzymes: Biological Catalysts Enzymes are biological catalysts, highly specific for their substrates. Substrates bind to the active site, where catalysis takes place, forming an enzyme– substrate complex. Review Figure 6.136.1324

25 Chapter 6: Energy, Enzymes, and Metabolism 6.13 Figure 6.13 figure 06-13.jpg

26 Chapter 6: Energy, Enzymes, and Metabolism Enzymes: Biological Catalysts At the active site, a substrate can be oriented correctly, chemically modified, or strained.At the active site, a substrate can be oriented correctly, chemically modified, or strained. As a result, the substrate readily forms its transition state, and the reaction proceeds.As a result, the substrate readily forms its transition state, and the reaction proceeds. Review Figures 6.14, 6.15 6.146.156.146.1526

27 Chapter 6: Energy, Enzymes, and Metabolism 6.14 Figure 6.14 figure 06-14.jpg

28 Chapter 6: Energy, Enzymes, and Metabolism 6.15 Figure 6.15 figure 06-15.jpg

29 Chapter 6: Energy, Enzymes, and Metabolism Enzymes: Biological Catalysts Substrate concentration affects the rate of an enzyme-catalyzed reaction. Review Figure 6.166.1629

30 Chapter 6: Energy, Enzymes, and Metabolism 6.16 Figure 6.16 figure 06-16.jpg

31 Chapter 6: Energy, Enzymes, and Metabolism Molecular Structure Determines Enzyme Function The active site where substrate binds determines the specificity of an enzyme.The active site where substrate binds determines the specificity of an enzyme. Upon binding to substrate, some enzymes change shape, facilitating catalysis.Upon binding to substrate, some enzymes change shape, facilitating catalysis. Review Figures 6.13, 6.18 6.136.186.136.1831

32 Chapter 6: Energy, Enzymes, and Metabolism 6.18 Figure 6.18 figure 06-18.jpg

33 Chapter 6: Energy, Enzymes, and Metabolism Molecular Structure Determines Enzyme Function Some enzymes require cofactors for catalysis. Prosthetic groups are permanently bound to the enzyme. Coenzymes usually are not. They enter into the reaction as a “cosubstrate,” as they are changed by the reaction and released from the enzyme. Review Table 6.16.133

34 Chapter 6: Energy, Enzymes, and Metabolism Table 6.1 table 06-01.jpg

35 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes Metabolism is organized into pathways: the product of one reaction is a reactant for the next.Metabolism is organized into pathways: the product of one reaction is a reactant for the next. Each reaction is catalyzed by an enzyme.Each reaction is catalyzed by an enzyme.35

36 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes Enzyme activity is subject to regulation. Some compounds react irreversibly with them and reduce their catalytic activity. Others react reversibly, inhibiting enzyme action temporarily. A compound structurally similar to an enzyme’s normal substrate may inhibit enzyme action. Review Figures 6.20, 6.216.206.2136

37 Chapter 6: Energy, Enzymes, and Metabolism 6.20 Figure 6.20 figure 06-20.jpg

38 Chapter 6: Energy, Enzymes, and Metabolism 6.21 – Part 1 Figure 6.21 – Part 1 figure 06-21a.jpg

39 Chapter 6: Energy, Enzymes, and Metabolism 6.21 – Part 2 Figure 6.21 – Part 2 figure 06-21b.jpg

40 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes For allosteric enzymes, plots of reaction rate versus substrate concentration are sigmoidal, in contrast to plots of the same variables for non-allosteric enzymes. Review Figure 6.226.2240

41 Chapter 6: Energy, Enzymes, and Metabolism 6.22 Figure 6.22 figure 06-22.jpg

42 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes Allosteric inhibitors bind to a site different from the active site and stabilize the inactive form of the enzyme.Allosteric inhibitors bind to a site different from the active site and stabilize the inactive form of the enzyme. The multiple catalytic subunits of many allosteric enzymes interact cooperatively.The multiple catalytic subunits of many allosteric enzymes interact cooperatively. Review Figure 6.23 6.23 42

43 Chapter 6: Energy, Enzymes, and Metabolism 6.23 Figure 6.23 figure 06-23.jpg

44 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes The end product of a metabolic pathway may inhibit the allosteric enzyme that catalyzes the commitment step of the pathway. Review Figure 6.246.2444

45 Chapter 6: Energy, Enzymes, and Metabolism 6.24 Figure 6.24 figure 06-24.jpg

46 Chapter 6: Energy, Enzymes, and Metabolism Metabolism and the Regulation of Enzymes Enzymes are sensitive to their environment. Both pH and temperature affect enzyme activity. Review Figures 6.25, 6.266.256.2646

47 Chapter 6: Energy, Enzymes, and Metabolism 6.25 Figure 6.25 figure 06-25.jpg

48 Chapter 6: Energy, Enzymes, and Metabolism 6.26 Figure 6.26 figure 06-26.jpg


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