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BIOENERGETICS
Dr. Aileen B. Angcajas
Chemistry Department
Xavier University-Ateneo de Cagayan
Bioenergetics
Bioenergetics is the quantitative study of the energy transductions
(conversions of one form of energy to another) that occur in living cells &
of the nature & function of the chemical processes underlying these
transductions.
Bioenergetics includes:
1) the radiant energy of sunlight used in photosynthesis
2) electrical energy of nerve impulses
3) mechanical energy of muscle contractions
4) heat energy liberated by chemical reactions within cells, and
5) potential energy stored in “energy-rich” chemical bonds.
The major source of biological energy is the chemical reactions occurring
inside cells.
BIOCHEMISTRY II
Chemical reactions in a cell are governed by thermodynamics
• Thermodynamically unfavorable chemical reactions can be driven forward by
coupling with thermodynamically favorable reactions
• The cell uses multistep chemical reactions to extract energy and atomic &
molecular components (catabolism) and to construct necessary molecular
building blocks (anabolism)
• Metabolic pathways are carefully regulated (using various methods) to fulfill
cellular needs while minimizing 'wasteful’ or energetically costly processes
• Cellular energy is manifested almost exclusively as phosphorylated organic
molecules (e.g., ATP) and reduced coenzymes (e.g., NADH; FADH2)
Fundamental features & themes in metabolism
BIOCHEMISTRY II
Metabolism
Catabolism Anabolism
• larger molecules
are broken down
• releases energy
• larger molecules
are made
• requires energy
The sum of all chemical reactions involved in maintaining the dynamic
state of a cell or organism.
BIOCHEMISTRY II
Metabolism
What are the fundamental questions in biochemical
metabolism?
• How do cells extract energy and reducing power from their
environment?
• How do cells synthesize the building blocks of their
macromolecules?
BIOCHEMISTRY II
Anabolism provides the substances needed for cellular
growth and repair
Dehydration synthesis
• type of anabolic process
• used to make polysaccharides, triglycerides, and proteins
• produces water
Anabolism
BIOCHEMISTRY II
Anabolism
BIOCHEMISTRY II
Catabolism breaks down larger molecules into smaller ones
Hydrolysis
• a catabolic process
• used to decompose carbohydrates, lipids, and proteins
• water is used
• reverse of dehydration synthesis
Catabolism
BIOCHEMISTRY II
Catabolism
BIOCHEMISTRY II
Metabolism is the sum of catabolism and anabolism
oxidation and the
release of energy
Triglycerides Proteins
Fatty acids
and glycerol
Amino
Acids
Small
molecules
Anabolism
of proteins
beakdown
of larger
molecules
to smaller
ones
Some nutrients and
products of catabolism
Products of anabolism,
including proteins and
nucleic acids
Catabolism Excretion
energy and
reducing
agents
Monosac-
charides
Polysac-
charides
Excretion Anabolism
Catabolism Anabolism
BIOCHEMISTRY II
CO2 , O2 , N2 cycling in the biosphere
BIOCHEMISTRY II
catabolic vs. anabolic processes
BIOCHEMISTRY II
Cells and the Mitochondria
Animal cells have many components, each with specific functions.
BIOCHEMISTRY II
What is the first stage of catabolic process?
Digestion
• Food is broken down by hydrolysis of esters,
glycosides, and peptide in the digestive system
• Yields fatty acids, simple sugars, and amino acids
• Smaller molecules are degraded in cells to acetyl
groups attached to the large carrier molecule
coenzyme A
BIOCHEMISTRY II
Digestion of Carbohydrates
• Carbohydrates are the main source of energy in a diet; the
main dietary carbohydrates are:
▫ The polysaccharide starch.
▫ The disaccharides lactose and sucrose.
▫ The monosaccharides glucose and fructose.
BIOCHEMISTRY II
Digestion of Carbohydrates
Digestion of carbohydrates starts in the mouth:
• α-Amylase catalyzes the hydrolysis of α -1,4-glycosidic bonds
of starch and glycogen.
• β-Amylase catalyzes the hydrolysis of β-1,4-glycosidic bonds.
• Debranching enzymes catalyze the hydrolysis of β -1,6-
glycosidic bonds.
BIOCHEMISTRY II
Digestion of Carbohydrates
BIOCHEMISTRY II
Digestion of Fats
Fats are the most concentrated source of energy.
▫ Lipases, the enzymes that catalyze the hydrolysis of
lipids, are located in the small intestine.
▫ Bile salts, synthesized in the liver and stored in the
gallbladder, emulsify water-insoluble dietary fats so that
they can be acted upon by lipases.
BIOCHEMISTRY II
• Fats are hydrolyzed to fatty acids, and complex lipids to fatty
acids, alcohols (glycerol, ethanolamine, sphingosine), and
carbohydrates.
• The hydrolysis products are absorbed through the intestinal
walls.
Digestion of Fats
BIOCHEMISTRY II
Digestion of Proteins
Although dietary proteins can be used for energy, their
main use is to furnish amino acids from which the body
can synthesize its own proteins.
BIOCHEMISTRY II
Digestion of Proteins
• Digestion of proteins begins with cooking, which denatures
proteins and makes it easier for the digestive enzymes and
HCl of the stomach to hydrolyze them.
• Most protein digestion occurs in the small intestine.
• The 10 essential amino acids must be obtained from the diet.
• Complete protein: A dietary protein that contains all
essential amino acids.
BIOCHEMISTRY II
BIOCHEMISTRY II
Common catabolic pathway
The two parts to the common catabolic pathway:
• The citric acid cycle, also called the tricarboxylic acid (TCA)
or Krebs cycle.
• Electron transport chain and phosphorylation, together
called oxidative phosphorylation.
BIOCHEMISTRY II
Thermodynamic processes of biochemical interest
BIOCHEMISTRY II
For any process A <=> B
(under constant T & P)
Thermodynamics in Metabolism:
the central equation
BIOCHEMISTRY II
Thermodynamics: enthalpy & entropy
BIOCHEMISTRY II
BIOCHEMISTRY II
Thermodynamics in Metabolism
Thermodynamics: Linking free energy to Keq
BIOCHEMISTRY II
BIOCHEMISTRY II
BIOCHEMISTRY II
actual free energy changes
BIOCHEMISTRY II
BIOCHEMISTRY II
Four principal compounds participating in the
common catabolic pathway are:
• AMP, ADP, and ATP
• NAD+/NADH
• FAD/FADH2
• coenzyme A; abbreviated CoA or CoA-SH
Compounds in catabolic pathway
BIOCHEMISTRY II
Each ATP molecule has three parts:
• an adenine molecule
• a ribose molecule
• three phosphate molecules in a chain
Adenosine triphosphate (ATP)
BIOCHEMISTRY II
• third phosphate attached by high-energy bond
• when the bond is broken, energy is transferred
• when the bond is broken, ATP becomes ADP
• ADP becomes ATP through phosphorylation
• phosphorylation requires energy released from cellular
respiration
Adenosine triphosphate (ATP)
BIOCHEMISTRY II
-N-glycosidic bond
H
H
H
O
-
O-P-O-P-O-P-O-CH2
HO OH
N
N
N
N
NH2
phosphoric
anhydrides
phosphoric
ester
-D-ribofuranose
adenine
O-
O-
O-
H
O O O
Adenosine triphosphate (ATP)
BIOCHEMISTRY II
ATP reactions often involve an
intermediate transfer step
ATP participation in a
reaction is often depicted
in a single step; the
mechanistic reality is
frequently a two-step
process
BIOCHEMISTRY II
ATP and varieties of nucleophilic attack
BIOCHEMISTRY II
What are the metabolic uses of ATP?
• An endergonic reaction has a thermodynamic barrier in
addition to a kinetic barrier
• Enzymes can cut kinetic barriers only
• Combining the reaction with an exergonic process (hydrolysis
of ATP) converts the energetics of the total process
• The endergonic reaction is "coupled" to an energetically
favorable reaction so that the overall free-energy change for
the two reactions together is favorable
BIOCHEMISTRY II
• The formation of glucose phosphate from glucose and HPO4
2− is
energetically unfavorable: ΔG°' = +13.8 kJ/mol (3.3 kcal/mol)
• The formation of glucose phosphate from ATP is energetically favorable
by 16.7 kJ/mol (4.0 kcal/mol)
Phosphorylation of glucose
BIOCHEMISTRY II
ATP links anabolic and catabolic reaction
BIOCHEMISTRY II
Adenosine-based cofactors involved
in oxidation-reduction reactions
BIOCHEMISTRY II
NAD+/NADH2
Nicotinamide adenine dinucleotide (NAD+) is a biological oxidizing agent.
BIOCHEMISTRY II
BIOCHEMISTRY II
Stereospecificity of Dehydrogenases that Employ NAD+ or NADP+ as Coenzymes
FAD/FADH2
Flavin adenine dinucleotide (FAD) is also a biological oxidizing agent.
BIOCHEMISTRY II
Some Enzymes (Flavoproteins) That Employ Flavin Nucleotide Coenzymes
BIOCHEMISTRY II
CoenzymeA
• Coenzyme A (CoA) is an acetyl-carrying group.
• CoA is often written CoA-SH to emphasize the fact that it contains a
sulfhydryl group.
• The acetyl group of acetyl CoA is bound as a high-energy thioester.
CH3 -C-S-CoA
O
Acetyl coenzyme A
(An acyl CoA)
BIOCHEMISTRY II
• Like NAD+ and FAD, coenzyme A contains a unit of ADP.
• The vitamin part of coenzyme A is pantothenic acid.
CoenzymeA
BIOCHEMISTRY II
• Oxidation-reduction or redox reactions
• Oxidation – removal of electrons
 Decrease in potential energy
 Dehydrogenation – removal of hydrogens
 Liberated hydrogen transferred by coenzymes
 Nicotinamide adenine dinucleotide (NAD)
 Flavin adenine dinucleotide (FAD)
 Glucose is oxidized
• Reduction – addition of electrons
 Increase in potential energy
What happen during energy transfer?
BIOCHEMISTRY II
• Fate of glucose depends on needs of body cells
▫ ATP production or synthesis of amino acids, glycogen,
or triglycerides
• Glucose transporter (GluT) bring glucose into the cell
via facilitate diffusion
▫ Insulin causes insertion of more of these transporters,
increasing rate of entry into cells
▫ Glucose trapped in cells after being phosphorylated
Carbohydrate Metabolism
BIOCHEMISTRY II
Occurs in three series of reactions
1. Glycolysis
2. Citric acid cycle
3. Electron transport chain
Produces
• carbon dioxide
• water
• ATP (chemical energy)
• heat
Includes
• anaerobic reactions (without O2) - produce little ATP
• aerobic reactions (requires O2) - produce most ATP
Cellular Respiration
BIOCHEMISTRY II
1
NADH + 2 H+
GLYCOLYSIS
+ 2 H+
NADH
CO2
FORMATION
OF ACETYL
COENZYME A
KREBS
CYCLE
+ 6 H+
CO2
FADH2
NADH
2
4
6
2
ELECTRON
TRANSPORT
CHAIN
e–
e–
e–
32 or 34
O2
6
6
2
2
2
2
H2O
Electrons
2 Acetyl
coenzyme A
2 Pyruvic acid
1 Glucose
ATP
ATP ATP
2
3
4
Overview of Cellular Respiration
BIOCHEMISTRY II
Cellular respiration begins with Glycolysis
BIOCHEMISTRY II
References
Nelson, D.L., & Cox, M.M. (2008) Lehninger Principles of Biochemistry, 5th ed. W.H. Freeman & Company New York.
Appling,D.R.,Cahill,.S.J.,& Mathews,C.K. (2016) Biochemistry,Concepts and Connections,Global Ed. Pearson
Education Limited, England.
Denniston, K.J., Topping, G.G., & Caret, R.L. (2008) General, Organic, & Biochemistry, 7th ed. The McGraw- Hill Companies, Inc.
McMurry, J. & Castellion, M. E, (1999) Fundamentals of General, Organic, & Bioligical Chemistry, 4th ed. Prentice Hall, Upper Saddle
River, New Jersey.
Timberlake, K.C. (2012) Chemistry an Introduction to General, Organic, & Biological Chemistry, 5th ed. Harper Collins Publishers, Inc.
Mckee, T. & Mckee, J.R. (1999) Biochemistry An Introduction, 2nd ed. WCB/McGraw-Hill Companies, Inc.
Campbell, M.K., & Farrell, S.O. (2009) Biochemistry 4th ed. Thomson Asia Ple Ltd.
Palmer T. (1995) Understanding Enzymes, 3rd Ellis Horwood Limited
Stoker, Stephen H. (2015) Biochemistry, 2nd Ed. Cengage Learning Asia Pte Ltd
BIOCHEMISTRY II

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Bioenergetics.pdf

  • 1. BIOENERGETICS Dr. Aileen B. Angcajas Chemistry Department Xavier University-Ateneo de Cagayan
  • 2. Bioenergetics Bioenergetics is the quantitative study of the energy transductions (conversions of one form of energy to another) that occur in living cells & of the nature & function of the chemical processes underlying these transductions. Bioenergetics includes: 1) the radiant energy of sunlight used in photosynthesis 2) electrical energy of nerve impulses 3) mechanical energy of muscle contractions 4) heat energy liberated by chemical reactions within cells, and 5) potential energy stored in “energy-rich” chemical bonds. The major source of biological energy is the chemical reactions occurring inside cells. BIOCHEMISTRY II
  • 3. Chemical reactions in a cell are governed by thermodynamics • Thermodynamically unfavorable chemical reactions can be driven forward by coupling with thermodynamically favorable reactions • The cell uses multistep chemical reactions to extract energy and atomic & molecular components (catabolism) and to construct necessary molecular building blocks (anabolism) • Metabolic pathways are carefully regulated (using various methods) to fulfill cellular needs while minimizing 'wasteful’ or energetically costly processes • Cellular energy is manifested almost exclusively as phosphorylated organic molecules (e.g., ATP) and reduced coenzymes (e.g., NADH; FADH2) Fundamental features & themes in metabolism BIOCHEMISTRY II
  • 4. Metabolism Catabolism Anabolism • larger molecules are broken down • releases energy • larger molecules are made • requires energy The sum of all chemical reactions involved in maintaining the dynamic state of a cell or organism. BIOCHEMISTRY II
  • 5. Metabolism What are the fundamental questions in biochemical metabolism? • How do cells extract energy and reducing power from their environment? • How do cells synthesize the building blocks of their macromolecules? BIOCHEMISTRY II
  • 6. Anabolism provides the substances needed for cellular growth and repair Dehydration synthesis • type of anabolic process • used to make polysaccharides, triglycerides, and proteins • produces water Anabolism BIOCHEMISTRY II
  • 8. Catabolism breaks down larger molecules into smaller ones Hydrolysis • a catabolic process • used to decompose carbohydrates, lipids, and proteins • water is used • reverse of dehydration synthesis Catabolism BIOCHEMISTRY II
  • 10. Metabolism is the sum of catabolism and anabolism oxidation and the release of energy Triglycerides Proteins Fatty acids and glycerol Amino Acids Small molecules Anabolism of proteins beakdown of larger molecules to smaller ones Some nutrients and products of catabolism Products of anabolism, including proteins and nucleic acids Catabolism Excretion energy and reducing agents Monosac- charides Polysac- charides Excretion Anabolism Catabolism Anabolism BIOCHEMISTRY II
  • 11. CO2 , O2 , N2 cycling in the biosphere BIOCHEMISTRY II
  • 12. catabolic vs. anabolic processes BIOCHEMISTRY II
  • 13.
  • 14. Cells and the Mitochondria Animal cells have many components, each with specific functions. BIOCHEMISTRY II
  • 15. What is the first stage of catabolic process? Digestion • Food is broken down by hydrolysis of esters, glycosides, and peptide in the digestive system • Yields fatty acids, simple sugars, and amino acids • Smaller molecules are degraded in cells to acetyl groups attached to the large carrier molecule coenzyme A BIOCHEMISTRY II
  • 16. Digestion of Carbohydrates • Carbohydrates are the main source of energy in a diet; the main dietary carbohydrates are: ▫ The polysaccharide starch. ▫ The disaccharides lactose and sucrose. ▫ The monosaccharides glucose and fructose. BIOCHEMISTRY II
  • 17. Digestion of Carbohydrates Digestion of carbohydrates starts in the mouth: • α-Amylase catalyzes the hydrolysis of α -1,4-glycosidic bonds of starch and glycogen. • β-Amylase catalyzes the hydrolysis of β-1,4-glycosidic bonds. • Debranching enzymes catalyze the hydrolysis of β -1,6- glycosidic bonds. BIOCHEMISTRY II
  • 19. Digestion of Fats Fats are the most concentrated source of energy. ▫ Lipases, the enzymes that catalyze the hydrolysis of lipids, are located in the small intestine. ▫ Bile salts, synthesized in the liver and stored in the gallbladder, emulsify water-insoluble dietary fats so that they can be acted upon by lipases. BIOCHEMISTRY II
  • 20. • Fats are hydrolyzed to fatty acids, and complex lipids to fatty acids, alcohols (glycerol, ethanolamine, sphingosine), and carbohydrates. • The hydrolysis products are absorbed through the intestinal walls. Digestion of Fats BIOCHEMISTRY II
  • 21. Digestion of Proteins Although dietary proteins can be used for energy, their main use is to furnish amino acids from which the body can synthesize its own proteins. BIOCHEMISTRY II
  • 22. Digestion of Proteins • Digestion of proteins begins with cooking, which denatures proteins and makes it easier for the digestive enzymes and HCl of the stomach to hydrolyze them. • Most protein digestion occurs in the small intestine. • The 10 essential amino acids must be obtained from the diet. • Complete protein: A dietary protein that contains all essential amino acids. BIOCHEMISTRY II
  • 24. Common catabolic pathway The two parts to the common catabolic pathway: • The citric acid cycle, also called the tricarboxylic acid (TCA) or Krebs cycle. • Electron transport chain and phosphorylation, together called oxidative phosphorylation. BIOCHEMISTRY II
  • 25. Thermodynamic processes of biochemical interest BIOCHEMISTRY II
  • 26. For any process A <=> B (under constant T & P) Thermodynamics in Metabolism: the central equation BIOCHEMISTRY II
  • 27. Thermodynamics: enthalpy & entropy BIOCHEMISTRY II
  • 29. Thermodynamics: Linking free energy to Keq BIOCHEMISTRY II
  • 32. actual free energy changes BIOCHEMISTRY II
  • 34. Four principal compounds participating in the common catabolic pathway are: • AMP, ADP, and ATP • NAD+/NADH • FAD/FADH2 • coenzyme A; abbreviated CoA or CoA-SH Compounds in catabolic pathway BIOCHEMISTRY II
  • 35. Each ATP molecule has three parts: • an adenine molecule • a ribose molecule • three phosphate molecules in a chain Adenosine triphosphate (ATP) BIOCHEMISTRY II
  • 36. • third phosphate attached by high-energy bond • when the bond is broken, energy is transferred • when the bond is broken, ATP becomes ADP • ADP becomes ATP through phosphorylation • phosphorylation requires energy released from cellular respiration Adenosine triphosphate (ATP) BIOCHEMISTRY II
  • 38. ATP reactions often involve an intermediate transfer step ATP participation in a reaction is often depicted in a single step; the mechanistic reality is frequently a two-step process BIOCHEMISTRY II
  • 39. ATP and varieties of nucleophilic attack BIOCHEMISTRY II
  • 40. What are the metabolic uses of ATP? • An endergonic reaction has a thermodynamic barrier in addition to a kinetic barrier • Enzymes can cut kinetic barriers only • Combining the reaction with an exergonic process (hydrolysis of ATP) converts the energetics of the total process • The endergonic reaction is "coupled" to an energetically favorable reaction so that the overall free-energy change for the two reactions together is favorable BIOCHEMISTRY II
  • 41. • The formation of glucose phosphate from glucose and HPO4 2− is energetically unfavorable: ΔG°' = +13.8 kJ/mol (3.3 kcal/mol) • The formation of glucose phosphate from ATP is energetically favorable by 16.7 kJ/mol (4.0 kcal/mol) Phosphorylation of glucose BIOCHEMISTRY II
  • 42. ATP links anabolic and catabolic reaction BIOCHEMISTRY II
  • 43. Adenosine-based cofactors involved in oxidation-reduction reactions BIOCHEMISTRY II
  • 44. NAD+/NADH2 Nicotinamide adenine dinucleotide (NAD+) is a biological oxidizing agent. BIOCHEMISTRY II
  • 45. BIOCHEMISTRY II Stereospecificity of Dehydrogenases that Employ NAD+ or NADP+ as Coenzymes
  • 46. FAD/FADH2 Flavin adenine dinucleotide (FAD) is also a biological oxidizing agent. BIOCHEMISTRY II
  • 47. Some Enzymes (Flavoproteins) That Employ Flavin Nucleotide Coenzymes BIOCHEMISTRY II
  • 48. CoenzymeA • Coenzyme A (CoA) is an acetyl-carrying group. • CoA is often written CoA-SH to emphasize the fact that it contains a sulfhydryl group. • The acetyl group of acetyl CoA is bound as a high-energy thioester. CH3 -C-S-CoA O Acetyl coenzyme A (An acyl CoA) BIOCHEMISTRY II
  • 49. • Like NAD+ and FAD, coenzyme A contains a unit of ADP. • The vitamin part of coenzyme A is pantothenic acid. CoenzymeA BIOCHEMISTRY II
  • 50. • Oxidation-reduction or redox reactions • Oxidation – removal of electrons  Decrease in potential energy  Dehydrogenation – removal of hydrogens  Liberated hydrogen transferred by coenzymes  Nicotinamide adenine dinucleotide (NAD)  Flavin adenine dinucleotide (FAD)  Glucose is oxidized • Reduction – addition of electrons  Increase in potential energy What happen during energy transfer? BIOCHEMISTRY II
  • 51. • Fate of glucose depends on needs of body cells ▫ ATP production or synthesis of amino acids, glycogen, or triglycerides • Glucose transporter (GluT) bring glucose into the cell via facilitate diffusion ▫ Insulin causes insertion of more of these transporters, increasing rate of entry into cells ▫ Glucose trapped in cells after being phosphorylated Carbohydrate Metabolism BIOCHEMISTRY II
  • 52. Occurs in three series of reactions 1. Glycolysis 2. Citric acid cycle 3. Electron transport chain Produces • carbon dioxide • water • ATP (chemical energy) • heat Includes • anaerobic reactions (without O2) - produce little ATP • aerobic reactions (requires O2) - produce most ATP Cellular Respiration BIOCHEMISTRY II
  • 53. 1 NADH + 2 H+ GLYCOLYSIS + 2 H+ NADH CO2 FORMATION OF ACETYL COENZYME A KREBS CYCLE + 6 H+ CO2 FADH2 NADH 2 4 6 2 ELECTRON TRANSPORT CHAIN e– e– e– 32 or 34 O2 6 6 2 2 2 2 H2O Electrons 2 Acetyl coenzyme A 2 Pyruvic acid 1 Glucose ATP ATP ATP 2 3 4 Overview of Cellular Respiration BIOCHEMISTRY II
  • 54. Cellular respiration begins with Glycolysis BIOCHEMISTRY II
  • 55. References Nelson, D.L., & Cox, M.M. (2008) Lehninger Principles of Biochemistry, 5th ed. W.H. Freeman & Company New York. Appling,D.R.,Cahill,.S.J.,& Mathews,C.K. (2016) Biochemistry,Concepts and Connections,Global Ed. Pearson Education Limited, England. Denniston, K.J., Topping, G.G., & Caret, R.L. (2008) General, Organic, & Biochemistry, 7th ed. The McGraw- Hill Companies, Inc. McMurry, J. & Castellion, M. E, (1999) Fundamentals of General, Organic, & Bioligical Chemistry, 4th ed. Prentice Hall, Upper Saddle River, New Jersey. Timberlake, K.C. (2012) Chemistry an Introduction to General, Organic, & Biological Chemistry, 5th ed. Harper Collins Publishers, Inc. Mckee, T. & Mckee, J.R. (1999) Biochemistry An Introduction, 2nd ed. WCB/McGraw-Hill Companies, Inc. Campbell, M.K., & Farrell, S.O. (2009) Biochemistry 4th ed. Thomson Asia Ple Ltd. Palmer T. (1995) Understanding Enzymes, 3rd Ellis Horwood Limited Stoker, Stephen H. (2015) Biochemistry, 2nd Ed. Cengage Learning Asia Pte Ltd BIOCHEMISTRY II