bio 178 lecture 14 metabolism and respiration

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Page 1: Bio 178 Lecture 14 Metabolism and Respiration

Bio 178 Lecture 14Metabolism and Respiration

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Page 2: Bio 178 Lecture 14 Metabolism and Respiration

Reading

• Chapters 8 & 9

Quiz Material

• Questions on P 158 & 184

• Chapters 8 & 9 Quizzes on Text Website (www.mhhe.com/raven7)

Page 3: Bio 178 Lecture 14 Metabolism and Respiration

Outline• Energy and Metabolism

Enzymes (cntd.)

• Cellular Respiration

Page 4: Bio 178 Lecture 14 Metabolism and Respiration

Environmental Effects on Enzyme CatalysisAffected by anything that alters its 3D shape:pH, [salt], temperature, regulatory molecules

Temperature• Optimum Temperature

Temperature at which reaction rate is greatest.

• Below Optimum

Increasing temp increases substrate-enzyme collisions & can stress bonds.

Bonds not flexible to permit induced fit not optimum.

• Above Optimum

Denaturation.

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Effect of Temperature on Enzyme Catalysis

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Environmental Effects on Enzyme Catalysis

pH

• Optimum pH

pH at which reaction rate is greatest.

• Above/Below Optimum

Change in [H+] affects charge balance between charged amino acids, which affects intramolecular bonding.

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Effect of pH on Enzyme Catalysis

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Molecules that Regulate Enzyme Action1. InhibitorsBind to enzymes to decrease their activity.• Function Regulation of metabolic pathways, eg. Feedback inhibition.

• Inhibitory Mechanisms

(a) Competitive Inhibitors

Compete with the substrate for the active site.

(b) Noncompetitive Inhibitors

Bind to enzyme in a regulatory site other than the active site conformational change.

Eg. Allosteric site - “on/off switches”

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Mechanisms of Enzyme Inhibition

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Molecules that Regulate Enzyme Action

2. Activators

Bind to enzymes to increase their activity.

Usually bind to allosteric sites.

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Enzyme CofactorsNon-protein “helpers” that aid in some enzyme catalyzed reactions.

• How do they Work?

Draw electrons away from covalent bonds in the substrate weaken bonds.

• Inorganic Cofactors

Example - Metal ions like zinc, molybdenum, & manganese.

• Coenzymes

Non-protein organic cofactors, eg. Vitamins.

Page 12: Bio 178 Lecture 14 Metabolism and Respiration

Coenzymes and Redox ReactionsCoenzymes (electron acceptors) shuttle energy from one enzyme to the next - pass energy with pairs of electrons from one substrate to the next in a reaction series.

Example: Nicotinamide adenine dinucleotide (NAD+)• Composition

2 nucleotides (NMP + AMP).

• Functions of its constituent parts

AMP - Core (conformation recognized by enzyme)

NMP - Electron acceptor

• Reduction of NAD+

NAD+ + 2H NADH + H+ (2 electrons & 1 H+ transferred to NAD+)

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Structure of NAD+

Page 14: Bio 178 Lecture 14 Metabolism and Respiration

Biochemical Pathways - Metabolism

• Anabolic Reactions

Biosynthetic part of metabolism - Energy expended to synthesize materials.

• Catabolic Reactions

Part of metabolism involved in hydrolyzing macromolecules - usually harvest energy.

• Biochemical Pathways

Sequences in which the products of one enzyme controlled reaction are the substrates for the next in a series of reactions.

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Biochemical Pathways

McGraw-Hill Video

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Regulation of Biochemical Pathways

• Why Regulate?

Save energy when a product is not needed.

• How is Regulation Achieved?

Feedback inhibition.

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Feedback inhibition

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Feedback Inhibition

McGraw-Hill Video

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How do Organisms Obtain Energy?

• Chemical bonds contain energy - these bonds must be broken to extract the energy.

• Energy (potential) is obtained from the electrons in the bond.

Step 1 - Digestion

Enzymes break the large molecules into smaller ones.

Step 2 - Catabolism

Enzymes break down the smaller molecules step by step, harvesting energy at each step.

Page 21: Bio 178 Lecture 14 Metabolism and Respiration

Cellular Respiration

The metabolic harvesting of energy by oxidation. The electrons (& the energy) are transferred from one molecule to the next, losing energy as they go.

Types of Cellular Respiration• Aerobic

Final electron acceptor is oxygen.

• Anaerobic

Final electron acceptor is an inorganic molecule other than oxygen.

• Fermentation

Final electron acceptor is an organic molecule.

Page 22: Bio 178 Lecture 14 Metabolism and Respiration

Cellular Respiration (Cntd.)

• Overall Reaction

C6H12O6 + 6O2 6CO2 + 6H2O + Energy

• ∆G-720 kcal/mole of glucose (cellular conditions)

Negative sign: Products contain less energy than reactants.

• Where does the Energy Released Go?

Cells harvest some of it to make ATP.

The rest is released as heat.

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Using ATP to Provide Energy

How is energy released from ATP?

The transfer of a phosphate group to another molecule relaxes the ATP (electrostatic repulsion).

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ATP Synthase

Makes most of the ATP produced by the cell.

What is the energy source for ATP synthase?

• Protons diffuse into the cell through ATP synthase.

• This releases energy.

• The energy is used by ATP synthase to rotate.

• This mechanical energy is converted to chemical energy by adding a third phosphate to ADP.

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ATP Synthase

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Glucose Catabolism

Methods for Making ATP

1. Substrate-Level Phosphorylation

ADP + Pi ATP

Pi comes from a phosphate bearing intermediate molecule.

Example - Glycolysis.

2. Aerobic Respiration

ATP synthase makes ATP using energy provided by electron transfer. O2 = final electron acceptor.

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Substrate-Level Phosphorylation

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Aerobic Respiration

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Processes Involved in Eukaryotic Respiration1. GlycolysisSugar splitting anaerobic process.

• Location

Cytoplasm

• Energetic Products2 ATP net & 2 NADH net produced by substrate level phosphorylation.

2. Aerobic Respiration• Pyruvate oxidation

• Krebs cycle

• Electron transport chain