Microbial Metabolism. PowerPoint Lecture Presentations prepared by Bradley W. Christian, McLennan Community College C H A P T E R

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1 PowerPoint Lecture Presentations prepared by Bradley W. Christian, McLennan Community College C H A P T E R 5 Microbial Metabolism

2 Big Picture: Metabolism Metabolism is the buildup and breakdown of nutrients within a cell These chemical reactions provide energy and create substances that sustain life

3 Big Picture pg. 108 (4 of 7).

4 Catabolic and Anabolic Reactions Catabolism: breaks down complex molecules; provides energy and building blocks for anabolism; exergonic Anabolism: uses energy and building blocks to build complex molecules; endergonic

5 Figure 5.1 The role of ATP in coupling anabolic and catabolic reactions.

6 Catabolic and Anabolic Reactions Metabolic pathways are sequences of enzymatically catalyzed chemical reactions in a cell Metabolic pathways are determined by enzymes Enzymes are encoded by genes

7 Collision Theory The collision theory states that chemical reactions occur when atoms, ions, and molecules collide Activation energy is the collision energy required for a chemical reaction to occur Reaction rate is the frequency of collisions containing enough energy to bring about a reaction Reaction rate can be increased by enzymes or by increasing temperature, pressure, or concentration

8 Enzymes and Chemical Reactions Catalysts speed up chemical reactions without being altered Enzymes are biological catalysts Enzymes act on a specific substrate and lower the activation energy

9 Figure 5.2 Energy requirements of a chemical reaction. Reaction without enzyme Activation energy without enzyme Reactant Reaction with enzyme Activation energy with enzyme Initial energy level Final energy level Products

10 Enzymes and Chemical Reactions Substrate contacts the enzyme's active site to form an enzyme-substrate complex Substrate is transformed and rearranged into products, which are released from the enzyme Enzyme is unchanged and can react with other substrates

11 Figure 5.3a The mechanism of enzymatic action. Substrate Active site Products Enzyme Enzyme substrate complex

12 Enzyme Specificity and Efficiency Enzymes have specificity for particular substrates Turnover number is the number of substrate molecules an enzyme converts to a product per second Generally 1 to 10,000

13 Naming Enzymes Names of enzymes usually end in ase; grouped based on the reaction they catalyze Oxidoreductase: oxidation-reduction reactions Transferase: transfer functional groups Hydrolase: hydrolysis Lyase: removal of atoms without hydrolysis Isomerase: rearrangement of atoms Ligase: joining of molecules; uses ATP

14 Figure 5.4 Components of a holoenzyme. Coenzyme Substrate Apoenzyme (protein portion), inactive Cofactor (nonprotein portion), activator Holoenzyme (whole enzyme), active

15 Factors Influencing Enzyme Activity Temperature ph Substrate concentration Inhibitors

16 Factors Influencing Enzyme Activity High temperature and extreme ph denature proteins If the concentration of substrate is high (saturation), the enzyme catalyzes at its maximum rate

17 Figure 5.6 Denaturation of a protein.

18 Figure 5.5a Factors that influence enzymatic activity, plotted for a hypothetical enzyme.

19 Figure 5.5b Factors that influence enzymatic activity, plotted for a hypothetical enzyme.

20 Figure 5.5c Factors that influence enzymatic activity, plotted for a hypothetical enzyme.

21 Inhibitors Competitive inhibitors fill the active site of an enzyme and compete with the substrate

22 Figure 5.7a-b Enzyme inhibitors. Normal Binding of Substrate Substrate Active site Action of Enzyme Inhibitors Competitive inhibitor Enzyme

23 Unnumbered Figure pg. 115 Sulfa drugs(sulfanilamide) competitive inhibitors for PABA (paraaminobenzoic acid), essential nutrient to synthesize folic acid.

24 Inhibitors Noncompetitive inhibitors interact with another part of the enzyme (allosteric site) rather than the active site in a process called allosteric inhibition

25 Figure 5.7a-c Enzyme inhibitors. Normal Binding of Substrate Substrate Active site Action of Enzyme Inhibitors Altered active site Enzyme Noncompetitive inhibitor Allosteric site

26 Feedback Inhibition End-product of a reaction allosterically inhibits enzymes from earlier in the pathway

27 Oxidation-Reduction Reactions Oxidation: removal of electrons Reduction: gain of electrons Redox reaction: an oxidation reaction paired with a reduction reaction

28 Oxidation-Reduction Reactions In biological systems, electrons and protons are removed at the same time; equivalent to a hydrogen atom Biological oxidations are often dehydrogenations

29 Figure 5.10 Representative biological oxidation. Ex. glucose Reduction H H + (proton) dehydrogenation Organic molecule that includes two hydrogen atoms (H) NAD + coenzyme (electron carrier) Oxidized organic molecule NADH + H + (proton) (reduced electron carrier) Oxidation

30 The Generation of ATP ATP is generated by the phosphorylation of ADP with the input of energy

31 Substrate-Level Phosphorylation ATP generated when high-energy PO 4 added to ADP generates ATP

32 Oxidative Phosphorylation Electrons are transferred from one electron carrier to another along an electron transport chain (system) on a membrane that releases energy to generate ATP

33 Photophosphorylation Occurs only in light-trapping photosynthetic cells Light energy is converted to ATP when the transfer of electrons (oxidation) from chlorophyll pass through a system of carrier molecules

34 Metabolic Pathways of Energy Production Series of enzymatically catalyzed chemical reactions Extracts energy from organic compounds and stores it in chemical form (ATP)

35 Carbohydrate Catabolism The breakdown of carbohydrates to release energy Glycolysis Krebs cycle Electron transport chain (system)

36 Glycolysis The oxidation of glucose to pyruvic acid produces ATP and NADH

37 Glycolysis The oxidation of glucose to pyruvic acid produces ATP and NADH Preparatory stage 2 ATP are used Glucose is split to form two molecules of glyceraldehyde 3-phosphate Energy-conserving stage The two glyceraldehyde 3-phosphate molecules are oxidized to 2 pyruvic acid molecules 4 ATP are produced ß remember 2 ATP were used during prep stage so 2 ATPs net gain for each glucose 2 NADH are produced

38 Figure 5.12 An outline of the reactions of glycolysis (Embden-Meyerhof pathway). 2 ATPs used 4 ATPs made 2 ATPs net

39 Additional Pathways to Glycolysis Pentose phosphate pathway Uses pentoses and produces NADPH Operates simultaneously with glycolysis Entner-Doudoroff pathway Produces NADPH and ATP Does not involve glycolysis Occurs in Pseudomonas, Rhizobium, and Agrobacterium

40 Cellular Respiration Oxidation of molecules liberates electrons to operate an electron transport chain Final electron acceptor comes from outside the cell and is inorganic ATP is generated by oxidative phosphorylation

41 Aerobic Respiration Krebs cycle Pyruvic acid (from glycolysis) is oxidized and decarboxylation (loss of CO 2 ) occurs The resulting two-carbon compound attaches to coenzyme A, forming acetyl CoA and NADH

42 Aerobic Respiration Krebs cycle (cont'd) Oxidation of acetyl CoA produces NADH, FADH 2, and ATP, and liberates CO 2 as waste 8 NADH per glucose = 24 ATP 2 FADH 2 per glucose = 4 ATP 2 GDP = 2 ATP From glycolysis 2 ATP net. = 2 ATP 2 NADH per glucose = 6 ATP In total - 38 ATPs

43 Figure 5.13 The Krebs cycle. Decarboxylation

44 Aerobic Respiration Electron transport chain (system) Occurs in the plasma membrane of prokaryotes; inner mitochondrial membrane of eukaryotes Series of carrier molecules (flavoproteins, cytochromes, and ubiquinones) are oxidized and reduced as electrons are passed down the chain Energy released is used to produce ATP by chemiosmosis

45 Figure 5.14 An electron transport chain (system). 2 NADHs from glycolysis 8 NADHs from TCA 2 FADH 2 s from TCA Cyanide binds with Fe in Cyt c and disrupts electron transport chain.

46 Aerobic Respiration Chemiosmosis Electrons (from NADH) pass down the electron transport chain while protons are pumped across the membrane Establishes proton gradient (proton motive force) Protons in higher concentration on one side of the membrane diffuse through ATP synthase Releases energy to synthesize ATP

47 Carbohydrate Catabolism Each NADH can be oxidized in the electron transport chain to produce 3 molecules of ATP Each FADH 2 can produce 2 molecules of ATP

48 Figure 5.16 Electron transport and the chemiosmotic generation of ATP.

49 Figure 5.15 Chemiosmosis.

50 Aerobic Respiration The final electron acceptor in the electron transport chain is molecular oxygen (O 2 )

51 Anaerobic Respiration The final electron acceptor in the electron transport chain is NOT O 2 Yields less energy than aerobic respiration

52 Anaerobic Respiration NO 3 Electron Acceptor NO 2, N 2 + H 2 O Products SO 4 H 2 S + H 2 O CO 3 2 CH 4 + H 2 O

53 Table 5.3 ATP Yield during Prokaryotic Aerobic Respiration of One Glucose Molecule

54 Fermentation Releases energy from the oxidation of organic molecules Does not require oxygen Does not use the Krebs cycle or ETC Uses an organic molecule as the final electron acceptor Produces only small amounts of ATP

55 Figure 5.18a Fermentation.

56 Fermentation Lactic acid fermentation: produces lactic acid Homolactic fermentation: produces lactic acid only Heterolactic fermentation: produces lactic acid and other compounds Glucose is oxidized to pyruvic acid, which is then reduced by NADH

57 Fermentation Alcohol fermentation: produces ethanol + CO 2 Glucose is oxidized to pyruvic acid; pyruvic acid is converted to acetaldehyde and CO 2 ; NADH reduces acetaldehyde to ethanol

58 Figure 5.19 Types of fermentation.

59 Figure 5.18b Fermentation. Glucose (glycolysis)

60 Table 5.4 Some Industrial Uses for Different Types of Fermentations*

61 Figure 5.11 An Overview of Respiration and Fermentation. 38 ATP 2 ATP

62 Lipid and Protein Catabolism Protein Extracellular proteases Amino acids Deamination, decarboxylation, dehydrogenation, desulfurization Organic acid Krebs cycle

63 Figure 5.20 Lipid catabolism.

64 Figure 5.21 Catabolism of various organic food molecules.

65 Biochemical Tests and Bacterial Identification Biochemical tests identify bacteria by detecting enzymes (e.g., those involved in decarboxylation and dehydrogenation)

66 Figure 5.22 Detecting amino acid catabolizing enzymes in the lab.

67 Biochemical Tests and Bacterial Identification Fermentation test: bacteria that catabolize carbohydrate or protein produce acid, causing the ph indicator to change color Oxidase test: identifies bacteria that have cytochrome oxidase (e.g., Pseudomonas)

68 Figure 5.23 A fermentation test. Mannitol with ph indicator and Durham tube

69 Chemoautotrophs Use energy from inorganic chemicals; CO 2 as carbon source Energy is used in the Calvin-Benson cycle to fix CO 2

70 Chemoheterotrophs Use energy and carbon from organic chemicals Glucose NAD + ETC Pyruvic acid NADH ADP + P ATP Medically and economically important

71 Metabolic Diversity among Organisms Nutritional Type Energy Source Carbon Source Example Photoautotroph Light CO 2 Oxygenic: Cyanobacteria, plants Anoxygenic: Green bacteria, purple bacteria Photoheterotroph Light Organic compounds Green bacteria, purple nonsulfur bacteria Chemoautotroph Inorganic Chemical CO 2 Iron-oxidizing bacteria Chemoheterotroph Chemical Organic compounds Fermentative bacteria Animals, protozoa, fungi, bacteria

72 Figure 5.29 The biosynthesis of polysaccharides.

73 Figure 5.30 The biosynthesis of simple lipids.

74 Figure 5.31a The biosynthesis of amino acids.

75 Figure 5.31b The biosynthesis of amino acids.

76 Figure 5.32 The biosynthesis of purine and pyrimidine nucleotides.

77 Check Your Understanding ü Where do amino acids required for protein synthesis come from? 5-24

78 The Integration of Metabolism Amphibolic pathways: metabolic pathways that function in both anabolism and catabolism Many pathways function simultaneously with common intermediates

79 Figure 5.33 The integration of metabolism.

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