导图社区 Chapter 8
- 30
- 0
- 0
- 举报
Chapter 8
关于Chapter 8的思维导图： An Introduction to Microbial Metabolism The Metabolism of Microbes Metabolism – all chemical and physical workings of a cell ...
编辑于2023-04-05 12:18:53 河南
- 相似推荐
- 大纲
Chapter 8
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
dtgdghd Macro
*/
function dtgdghd()
{Function SlideShowWindows
}Float64Array
Debug
SaveSetting
Symbol
key word generation
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions
Chapter 8
An Introduction to Microbial Metabolism
The Metabolism of Microbes
Metabolism – all chemical and physical workings of a cell
Two types of chemical reactions:
Catabolism – degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy
Anabolism – biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input
Enzymes
Enzymes are biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation (the resistance to a reaction)
The enzyme is not permanently altered in the reaction
Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position
Enzyme Structure
Simple enzymes – consist of protein alone
Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules
Apoenzyme – protein portion
Cofactors – nonprotein portion
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins
Enzyme Examples and their Cofactors
Apoenzymes: Specificity and the Active Site
Exhibits primary, secondary, tertiary, and some, quaternary structure
Site for substrate binding is active site, or catalytic site
Apoenzymes: Specificity and the Active Site
A temporary enzyme-substrate union occurs when substrate moves into active site – induced fit
Appropriate reaction occurs; product is formed and released
Cofactors: Supporting the Work of Enzymes
Micronutrients are needed as cofactors
Cofactors act as carriers to assist the enzyme in its activity
Location of Enzyme Action
Exoenzymes – transported extracellularly, where they break down large food molecules or harmful chemicals
Cellulase, amylase, penicillinase
Endoenzymes – retained intracellularly and function there
Most enzymes are endoenzymes
Constitutive enzymes – always present, always produced in equal amounts or at equal rates, regardless of the amount of substrate
Regulated enzymes – not constantly present; production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration
Synthesis and Hydrolysis Reactions
Synthesis or condensation reactions – anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed
Synthesis and Hydrolysis Reactions
Hydrolysis reactions – catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by the cell’s environment
Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat
When enzymes are subjected to changes in organism’s habitat they become unstable
Labile: chemically unstable enzymes
Denaturation: weak bonds that maintain the shape of the apoenzyme are broken
Direct Controls on the Actions of Enzymes
Competitive inhibition – substance that resembles the normal substrate competes with the substrate for the active site
Noncompetitive inhibition – enzymes are regulated by the binding of molecules other than the substrate away from the active site
Enzyme repression – inhibits at the genetic level by controlling synthesis of key enzymes
Enzyme induction – enzymes are made only when suitable substrates are present
Regulation of enzyme action
Enzyme repression
Overview of Enzyme Characteristics
The Pursuit and Utilization of Energy
Energy: the capacity to do work or to cause change
Forms of energy include
Thermal, radiant, electrical, mechanical, atomic, and chemical
Cell Energetics
Cells manage energy in the form of chemical reactions that make or break bonds and transfer electrons
Endergonic reactions – consume energy
Exergonic reactions – release energy
Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Biological Oxidation and Reduction
Redox reactions – always occur in pairs
There is an electron donor and electron acceptor which constitute a redox pair
Process salvages electrons and their energy
Released energy can be captured to phosphorylate ADP or another compound
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy
Most carriers are coenzymes:
NAD, FAD, NADP, coenzyme A, and compounds of the respiratory chain
Adenosine Triphosphate: ATP
Metabolic “currency”
Three part molecule consisting of:
Adenine – a nitrogenous base
Ribose – a 5-carbon sugar
3 phosphate groups
Removal of the terminal phosphate releases energy
ATP utilization and replenishment is a constant cycle in active cells
Phosphorylation of Glucose by ATP
Formation of ATP
ATP can be formed by three different mechanisms:
Substrate-level phosphorylation – transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP
Oxidative phosphorylation – series of redox reactions occurring during respiratory pathway
Photophosphorylation – ATP is formed utilizing the energy of sunlight
Pathways of Bioenergetics
Bioenergetics – study of the mechanisms of cellular energy release
Includes catabolic and anabolic reactions
Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
Glycolysis
Kreb’s cycle
Respiratory chain, electron transport
Metabolic Strategies
Nutrient processing is varied, yet in many cases is based on three catabolic pathways that convert glucose to CO2 and gives off energy
Aerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain
Anaerobic respiration – glycolysis, the Kreb’s cycle, respiratory chain; molecular oxygen is not the final electron acceptor
Fermentation – glycolysis, organic compounds are the final electron acceptors
Overview of Catabolic Pathways
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor
Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated
TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated
Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation
Glycolysis
Fate of Pyruvate
Krebs Cycle
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP
Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2)
ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation
Electron Transport and Chemiosmosis
The Formation of ATP and Chemiosmosis
Chemiosmosis – as the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force
Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-D change resulting in the production of ATP
Electron Transport and ATP Synthesis in Bacterial Cell Envelope
The Terminal Step
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor
2H+ + 2e- + ½O2 → H2O
Theoretic ATP Yield for Aerobic Respiration
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor
Nitrate (NO3-) and nitrite (NO2-)
Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as terminal electron acceptors
Yields a small amount of ATP
Production of ethyl alcohol by yeasts acting on glucose
Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid
Alcoholic & Acidic Fermentation
Products of Pyruvate Fermentation
Comparing Aerobic Respiration, Fermentation and Anaerobic Respiration
Biosynthesis and the Crossing Pathways of Metabolism
Many pathways of metabolism are bi-directional or amphibolic
Biosynthesis and the Crossing Pathways of Metabolism
Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways
Reactions that produce and convert amino acids
Photosynthesis: The Earth’s Lifeline
The ultimate source of all the chemical energy in cells comes from the sun
6CO2 + 6H2O C6H12O6 + 6O2
Photosynthesis
Occurs in 2 stages:
Light-dependent – photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments
Water split by photolysis, releasing O2 gas and provides electrons to drive photophosphorylation
Released light energy used to synthesize ATP and NADPH
Photosynthesis
Occurs in 2 stages:
Light-dependent
Light-independent reaction – dark reactions – Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose
Photosynthesis Reactions
Calvin Cycle Reactions