AP BIO: Semester 1 FERP Unit 3
This is a comprehensive list of key concepts and questions from AP Biology Unit 3: Cellular Energetics. Below are simplified answers to some of the questions for clarity and quick reference:
Monomer of an enzyme: Amino acids are the monomers that make up enzymes (proteins).
How a substrate binds: Substrates bind to an enzyme's active site, which has a specific shape complementary to the substrate.
After substrate binds: The enzyme changes shape slightly (induced fit), facilitating the reaction and converting the substrate into the product.
Function of an enzyme: Enzymes speed up biological reactions by lowering activation energy.
True/False (Gibbs Free Energy): False – Enzymes do not affect Gibbs Free Energy; they only lower the activation energy.
Enzyme's effect on reaction rate: Enzymes increase the reaction rate by providing an alternative pathway with lower activation energy.
Activation energy (catalyzed vs. uncatalyzed): In an enzyme-catalyzed reaction, activation energy is lower.
Reaction rate (catalyzed vs. uncatalyzed): Catalyzed reactions occur much faster than uncatalyzed ones.
Conditions affecting enzyme structure: Temperature and pH.
Change in structure's effect: It alters the enzyme's ability to bind substrates (loss of function).
Outcomes of structural change:
Enzyme works less effectively.
Enzyme stops working entirely.
Enzyme regains function if the change is reversible.
Denaturation: Loss of an enzyme's functional shape due to environmental stress.
True/False (Reversibility): True – Some enzymes can regain their structure under the right conditions.
Reversible example: RNAse A.
Nonreversible example: Fried egg proteins.
Effect of hydrogen ions on pH:
Increase: pH decreases (more acidic).
Decrease: pH increases (more basic).
Effect of pH changes on enzyme:
Increase: Enzyme denatures if too basic.
Decrease: Enzyme denatures if too acidic.
Reactant concentration on rate: Higher concentrations increase reaction rate up to a saturation point.
Enzyme concentration on rate: Higher enzyme levels increase reaction rate, provided substrates are available.
Temperature effects:
Increase: Molecules move faster, but extreme heat denatures enzymes.
Decrease: Molecules move slower, reducing reaction rate.
Temperature on molecules: Affects kinetic energy and collision frequency.
Competitive inhibitor: Molecule competes with the substrate for the active site.
Overcoming competitive inhibitor: Increase substrate concentration.
Noncompetitive inhibitor: Binds elsewhere on the enzyme, changing its shape.
Inhibitor's effect on reaction rate: Slows down the reaction rate.
First Law of Thermodynamics: Energy cannot be created or destroyed, only transformed.
Second Law of Thermodynamics: Energy transfers increase the universe's entropy.
Maintaining order: Requires energy input.
Powering cellular processes: ATP (adenosine triphosphate).
Endergonic reaction: Absorbs energy (e.g., photosynthesis).
Exergonic reaction: Releases energy (e.g., cellular respiration).
Energy coupling: Uses energy from exergonic reactions to power endergonic reactions.
Energy source: Light.
First photosynthetic organism: Cyanobacteria.
Oxygenation evidence: Banded iron formations in ancient rocks.
Light-dependent reactions: Convert light energy to ATP and NADPH.
Location: Thylakoid membranes of chloroplasts.
ATP synthesis: Proton gradient powers ATP synthase.
NADPH synthesis: Light excites electrons, which reduce NADP+ to NADPH.
Chlorophyll: Pigment capturing light energy.
Photosystem and electron transport chain: Photosystem absorbs light, exciting electrons that move through the ETC.
Processes: Glycolysis, Citric Acid Cycle (Krebs), Electron Transport Chain.
Products: ATP, CO₂, and water.
Electron transport chain (ETC): Series of proteins transferring electrons to create a proton gradient.
ETC locations:
Mitochondrial inner membrane (eukaryotes).
Plasma membrane (prokaryotes).
Pathway of electrons:
Start: Glucose.
Carriers: NADH and FADH₂.
End: Oxygen (final acceptor).
Proton gradient generation: From ETC using energy from electrons.
Proton direction (ETC): Pumped from matrix to intermembrane space (mitochondria).
Chemiosmosis: Proton flow through ATP synthase drives ATP production.
Oxidative phosphorylation: ATP synthesis using oxygen and ETC.
Photophosphorylation: ATP synthesis in photosynthesis using light energy.
Endotherm: Maintains body temperature through internal mechanisms (e.g., metabolism).
Decoupling oxidative phosphorylation: Generates heat by uncoupling proton gradient from ATP synthesis.
This is a comprehensive list of key concepts and questions from AP Biology Unit 3: Cellular Energetics. Below are simplified answers to some of the questions for clarity and quick reference:
Monomer of an enzyme: Amino acids are the monomers that make up enzymes (proteins).
How a substrate binds: Substrates bind to an enzyme's active site, which has a specific shape complementary to the substrate.
After substrate binds: The enzyme changes shape slightly (induced fit), facilitating the reaction and converting the substrate into the product.
Function of an enzyme: Enzymes speed up biological reactions by lowering activation energy.
True/False (Gibbs Free Energy): False – Enzymes do not affect Gibbs Free Energy; they only lower the activation energy.
Enzyme's effect on reaction rate: Enzymes increase the reaction rate by providing an alternative pathway with lower activation energy.
Activation energy (catalyzed vs. uncatalyzed): In an enzyme-catalyzed reaction, activation energy is lower.
Reaction rate (catalyzed vs. uncatalyzed): Catalyzed reactions occur much faster than uncatalyzed ones.
Conditions affecting enzyme structure: Temperature and pH.
Change in structure's effect: It alters the enzyme's ability to bind substrates (loss of function).
Outcomes of structural change:
Enzyme works less effectively.
Enzyme stops working entirely.
Enzyme regains function if the change is reversible.
Denaturation: Loss of an enzyme's functional shape due to environmental stress.
True/False (Reversibility): True – Some enzymes can regain their structure under the right conditions.
Reversible example: RNAse A.
Nonreversible example: Fried egg proteins.
Effect of hydrogen ions on pH:
Increase: pH decreases (more acidic).
Decrease: pH increases (more basic).
Effect of pH changes on enzyme:
Increase: Enzyme denatures if too basic.
Decrease: Enzyme denatures if too acidic.
Reactant concentration on rate: Higher concentrations increase reaction rate up to a saturation point.
Enzyme concentration on rate: Higher enzyme levels increase reaction rate, provided substrates are available.
Temperature effects:
Increase: Molecules move faster, but extreme heat denatures enzymes.
Decrease: Molecules move slower, reducing reaction rate.
Temperature on molecules: Affects kinetic energy and collision frequency.
Competitive inhibitor: Molecule competes with the substrate for the active site.
Overcoming competitive inhibitor: Increase substrate concentration.
Noncompetitive inhibitor: Binds elsewhere on the enzyme, changing its shape.
Inhibitor's effect on reaction rate: Slows down the reaction rate.
First Law of Thermodynamics: Energy cannot be created or destroyed, only transformed.
Second Law of Thermodynamics: Energy transfers increase the universe's entropy.
Maintaining order: Requires energy input.
Powering cellular processes: ATP (adenosine triphosphate).
Endergonic reaction: Absorbs energy (e.g., photosynthesis).
Exergonic reaction: Releases energy (e.g., cellular respiration).
Energy coupling: Uses energy from exergonic reactions to power endergonic reactions.
Energy source: Light.
First photosynthetic organism: Cyanobacteria.
Oxygenation evidence: Banded iron formations in ancient rocks.
Light-dependent reactions: Convert light energy to ATP and NADPH.
Location: Thylakoid membranes of chloroplasts.
ATP synthesis: Proton gradient powers ATP synthase.
NADPH synthesis: Light excites electrons, which reduce NADP+ to NADPH.
Chlorophyll: Pigment capturing light energy.
Photosystem and electron transport chain: Photosystem absorbs light, exciting electrons that move through the ETC.
Processes: Glycolysis, Citric Acid Cycle (Krebs), Electron Transport Chain.
Products: ATP, CO₂, and water.
Electron transport chain (ETC): Series of proteins transferring electrons to create a proton gradient.
ETC locations:
Mitochondrial inner membrane (eukaryotes).
Plasma membrane (prokaryotes).
Pathway of electrons:
Start: Glucose.
Carriers: NADH and FADH₂.
End: Oxygen (final acceptor).
Proton gradient generation: From ETC using energy from electrons.
Proton direction (ETC): Pumped from matrix to intermembrane space (mitochondria).
Chemiosmosis: Proton flow through ATP synthase drives ATP production.
Oxidative phosphorylation: ATP synthesis using oxygen and ETC.
Photophosphorylation: ATP synthesis in photosynthesis using light energy.
Endotherm: Maintains body temperature through internal mechanisms (e.g., metabolism).
Decoupling oxidative phosphorylation: Generates heat by uncoupling proton gradient from ATP synthesis.