Chapter 3 Bioenergetics EXERCISE PHYSIOLOGY Theory and Application to Fitness and Performance, 6th...
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Transcript of Chapter 3 Bioenergetics EXERCISE PHYSIOLOGY Theory and Application to Fitness and Performance, 6th...
Chapter 3Bioenergetics
EXERCISE PHYSIOLOGYTheory and Application to Fitness and Performance,
6th edition
Scott K. Powers & Edward T. Howley
Introduction
• Metabolism – Sum of all chemical reactions that occur in the
body– Anabolic reactions
• Synthesis of molecules
– Catabolic reactions• Breakdown of molecules
• Bioenergetics– Converting foodstuffs (fats, proteins,
carbohydrates) into energy
Cell Structure
• Cell membrane– Semipermeable membrane that separates the
cell from the extracellular environment
• Nucleus– Contains genes that regulate protein synthesis
• Cytoplasm– Fluid portion of cell– Contains organelles
• Mitochondria
A Typical Cell and Its Major Organelles
Figure 3.1
Steps Leading to Protein Synthesis
Figure 3.2
Cellular Chemical Reactions
• Endergonic reactions– Require energy to be added
• Exergonic reactions– Release energy
• Coupled reactions– Liberation of energy in an exergonic reaction
drives an endergonic reaction
The Breakdown of Glucose: An Exergonic Reaction
Figure 3.3
Coupled Reactions
Figure 3.4
Oxidation-Reduction Reactions
• Oxidation – Removing an electron
• Reduction – Addition of an electron
• Oxidation and reduction are always coupled reactions• Often involves the transfer of hydrogen atoms rather than
free electrons– Hydrogen atom contains one electron– A molecule that loses a hydrogen also loses an electron
and therefore is oxidized
Oxidation-Reduction Reaction involving NAD and NADH
Figure 3.5
Enzymes
• Catalysts that regulate the speed of reactions– Lower the energy of activation
• Factors that regulate enzyme activity– Temperature– pH
• Interact with specific substrates– Lock and key model
Figure 3.6
Enzymes Catalyze Reactions
Figure 3.7
The Lock-and-Key Model of Enzyme Action
Table 3.1
Diagnostic Value of Measuring Enzyme Activity in the Blood
Enzyme Diseases Associated w/ High Blood Levels of Enzyme
Lactate dehydrogenase (Cardiac-specific isoform) Myocardial infarction
Creatin kinase Myocardial infarction, muscular dystrophy
Alkaline phosphatase Carcinoma of bone, Paget’s disease, obstructive jaundice
Amylase Pancreatitis, perforated peptic ulcer
Aldolase Muscular dystrophy
Classification of Enzymes
• Oxidoreductases– Catalyze oxidation-reduction reactions
• Transferases– Transfer elements of one molecule to another
• Hydrolases– Cleave bonds by adding water
• Lyases– Groups of elements are removed to form a double bond or added to
a double bond• Isomerases
– Rearrangement of the structure of molecules• Ligases
– Catalyze bond formation between substrate molecules
Example of the Major Classes of Enzymes
Example of Enzyme
Enzyme Class within this Class Reaction Catalyzed
Oxidoreducatases Lactate dehydrogenase Lactate + NAD <-->Pyruvate + NADH + H
Transferases Hexokinase Glucose + ATP Glucose 6-phosphate + ADP
Hydrolases Lipase Triglyceride + 3 H20 Glycerol + 3 Fatty acids
Lyases Carbonic anhydrase Carbon dioxide + H20 Carbonic acid
Isomerases Phosphoglycerate mutase 3-Phosphoglycerate 2-Phosphoglycerate
Ligases Pyruvate carboxylase Pyruvate + HC03 + ATP Oxaloacetate + ADP
Table 3.2
Factors That Alter Enzyme Activity
• Temperature– Small rise in body temperature increases
enzyme activity
• pH– Changes in pH reduces enzyme activity
The Effect of Body Temperature on Enzyme Activity
Figure 3.8
The Effect of pH on Enzyme Activity
Figure 3.9
Fuels for Exercise
• Carbohydrates – Glucose– Glycogen
• Storage form of glucose in liver and muscle
• Fats– Fatty acids– Triglycerides
• Storage form of fat in muscle and adipose tissue
• Proteins– Not a primary energy source during exercise
ADP + Pi ATP
• Adenosine triphosphate (ATP)– Consists of adenine, ribose, and three linked
phosphates
• Synthesis
• Breakdown
High-Energy Phosphates
ADP + Pi + EnergyATP ATPase
Figure 3.10
Structure of ATP
Figure 3.11
Model of ATP as the Universal Energy Donor
Bioenergetics
• Formation of ATP – Phosphocreatine (PC) breakdown– Degradation of glucose and glycogen
• Glycolysis– Oxidative formation of ATP
• Anaerobic pathways
– Do not involve O2
– PC breakdown and glycolysis• Aerobic pathways
– Require O2
– Oxidative phosphorylation
Anaerobic ATP Production
• ATP-PC system– Immediate source of ATP
• Glycolysis– Glucose 2 pyruvic acid or 2 lactic acid – Energy investment phase
• Requires 2 ATP
– Energy generation phase• Produces 4 ATP, 2 NADH, and 2 pyruvate or 2 lactate
ATP + CPC + ADPCreatine kinase
Figure 3.12
The Two Phases of Glycolysis
Figure 3.14
Interaction Between Blood Glucose and Muscle Glycogen in Glycolysis
Figure 3.15
Glycolysis: Energy Investment Phase
Figure 3.15
Glycolysis: Energy Generation Phase
Hydrogen and Electron Carrier Molecules
• Transport hydrogens and associated electrons– To mitochondria for ATP generation (aerobic)– To convert pyruvic acid to lactic acid (anaerobic)
• Nicotinamide adenine dinucleotide (NAD)
• Flavin adenine dinucleotide (FAD)
NAD + 2H+ NADH + H+
FAD + 2H+ FADH2
Figure 3.16
Conversion of Pyruvic Acid to Lactic Acid
Aerobic ATP Production
• Krebs cycle (citric acid cycle)– Completes the oxidation of substrates – Produces NADH and FADH to enter the electron
transport chain
• Electron transport chain – Oxidative phosphorylation– Electrons removed from NADH and FADH are
passed along a series of carriers to produce ATP– H+ from NADH and FADH are accepted by O2 to
form water
Figure 3.17
The Three Stages of Oxidative
Phosphorylation
The Krebs Cycle
Figure 3.18
Fats and Proteins in Aerobic Metabolism
• Fats– Triglycerides glycerol and fatty acids– Fatty acids acetyl-CoA
• Beta-oxidation
– Glycerol is not an important muscle fuel during exercise
• Protein– Broken down into amino acids– Converted to glucose, pyruvic acid, acetyl-CoA,
and Krebs cycle intermediates
Figure 3.19
Relationship Between the Metabolism of Proteins, Carbohydrates, and Fats
Figure 3.21
Beta-oxidation
The Electron Transport Chain
Figure 3.20
Metabolic Process High-Energy Products
ATP from Oxidative Phosphorylation
ATP Subtotal
Glycolysis 2 ATP 2 NADH
— 5
2 (if anaerobic) 7 (if aerobic)
Pyruvic acid to acetyl-CoA 2 NADH 5 12
Krebs cycle 2 GTP 6 NADH 2 FADH
— 15 3
14 29 32
Grand Total
32
Aerobic ATP Tally Per Glucose Molecule
Table 3.3
Efficiency of Oxidative Phosphorylation
• One mole of ATP has energy yield of 7.3 kcal• 32 moles of ATP are formed from one mole of glucose• Potential energy released from one mole of glucose is 686
kcal/mole• Overall efficiency of aerobic respiration is 34%
– 66% of energy released as heat
32 moles ATP/mole glucose x 7.3 kcal/mole ATP
686 kcal/mole glucosex 100 = 34%
Control of Bioenergetics
• Rate-limiting enzymes– An enzyme that regulates the rate of a metabolic
pathway
• Modulators of rate-limiting enzymes– Levels of ATP and ADP+Pi
• High levels of ATP inhibit ATP production
• Low levels of ATP and high levels of ADP+Pi stimulate ATP production
– Calcium may stimulate aerobic ATP production
Action of Rate-Limiting Enzymes
Figure 3.24
Interaction Between Aerobic and Anaerobic ATP Production
• Energy to perform exercise comes from an interaction between aerobic and anaerobic pathways
• Effect of duration and intensity– Short-term, high-intensity activities
• Greater contribution of anaerobic energy systems
– Long-term, low to moderate-intensity exercise• Majority of ATP produced from aerobic sources
Effect of Event Duration on the Contribution of Aerobic/Anaerobic ATP Production
Figure 3.24