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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:


Enzymes and Catalysis

  1. Monomer of an enzyme: Amino acids are the monomers that make up enzymes (proteins).

  2. How a substrate binds: Substrates bind to an enzyme's active site, which has a specific shape complementary to the substrate.

  3. After substrate binds: The enzyme changes shape slightly (induced fit), facilitating the reaction and converting the substrate into the product.

  4. Function of an enzyme: Enzymes speed up biological reactions by lowering activation energy.

  5. True/False (Gibbs Free Energy): False – Enzymes do not affect Gibbs Free Energy; they only lower the activation energy.

  6. Enzyme's effect on reaction rate: Enzymes increase the reaction rate by providing an alternative pathway with lower activation energy.

  7. Activation energy (catalyzed vs. uncatalyzed): In an enzyme-catalyzed reaction, activation energy is lower.

  8. Reaction rate (catalyzed vs. uncatalyzed): Catalyzed reactions occur much faster than uncatalyzed ones.


Environmental Impacts on Enzymes

  1. Conditions affecting enzyme structure: Temperature and pH.

  2. Change in structure's effect: It alters the enzyme's ability to bind substrates (loss of function).

  3. Outcomes of structural change:

    • Enzyme works less effectively.

    • Enzyme stops working entirely.

    • Enzyme regains function if the change is reversible.

  4. Denaturation: Loss of an enzyme's functional shape due to environmental stress.

  5. True/False (Reversibility): True – Some enzymes can regain their structure under the right conditions.

  6. Reversible example: RNAse A.

  7. Nonreversible example: Fried egg proteins.


pH and Temperature

  1. Effect of hydrogen ions on pH:

    • Increase: pH decreases (more acidic).

    • Decrease: pH increases (more basic).

  2. Effect of pH changes on enzyme:

    • Increase: Enzyme denatures if too basic.

    • Decrease: Enzyme denatures if too acidic.

  3. Reactant concentration on rate: Higher concentrations increase reaction rate up to a saturation point.

  4. Enzyme concentration on rate: Higher enzyme levels increase reaction rate, provided substrates are available.

  5. Temperature effects:

    • Increase: Molecules move faster, but extreme heat denatures enzymes.

    • Decrease: Molecules move slower, reducing reaction rate.

  6. Temperature on molecules: Affects kinetic energy and collision frequency.


Inhibitors

  1. Competitive inhibitor: Molecule competes with the substrate for the active site.

  2. Overcoming competitive inhibitor: Increase substrate concentration.

  3. Noncompetitive inhibitor: Binds elsewhere on the enzyme, changing its shape.

  4. Inhibitor's effect on reaction rate: Slows down the reaction rate.


Energy and Thermodynamics

  1. First Law of Thermodynamics: Energy cannot be created or destroyed, only transformed.

  2. Second Law of Thermodynamics: Energy transfers increase the universe's entropy.

  3. Maintaining order: Requires energy input.

  4. Powering cellular processes: ATP (adenosine triphosphate).

  5. Endergonic reaction: Absorbs energy (e.g., photosynthesis).

  6. Exergonic reaction: Releases energy (e.g., cellular respiration).

  7. Energy coupling: Uses energy from exergonic reactions to power endergonic reactions.


Photosynthesis

  1. Energy source: Light.

  2. First photosynthetic organism: Cyanobacteria.

  3. Oxygenation evidence: Banded iron formations in ancient rocks.

  4. Light-dependent reactions: Convert light energy to ATP and NADPH.

  5. Location: Thylakoid membranes of chloroplasts.

  6. ATP synthesis: Proton gradient powers ATP synthase.

  7. NADPH synthesis: Light excites electrons, which reduce NADP+ to NADPH.

  8. Chlorophyll: Pigment capturing light energy.

  9. Photosystem and electron transport chain: Photosystem absorbs light, exciting electrons that move through the ETC.


Cellular Respiration

  1. Processes: Glycolysis, Citric Acid Cycle (Krebs), Electron Transport Chain.

  2. Products: ATP, CO₂, and water.

  3. Electron transport chain (ETC): Series of proteins transferring electrons to create a proton gradient.

  4. ETC locations:

    • Mitochondrial inner membrane (eukaryotes).

    • Plasma membrane (prokaryotes).

  5. Pathway of electrons:

    • Start: Glucose.

    • Carriers: NADH and FADH₂.

    • End: Oxygen (final acceptor).

  6. Proton gradient generation: From ETC using energy from electrons.

  7. Proton direction (ETC): Pumped from matrix to intermembrane space (mitochondria).

  8. Chemiosmosis: Proton flow through ATP synthase drives ATP production.

  9. Oxidative phosphorylation: ATP synthesis using oxygen and ETC.

  10. Photophosphorylation: ATP synthesis in photosynthesis using light energy.


Organismal Fitness

  1. Endotherm: Maintains body temperature through internal mechanisms (e.g., metabolism).

  2. Decoupling oxidative phosphorylation: Generates heat by uncoupling proton gradient from ATP synthesis.


HP

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:


Enzymes and Catalysis

  1. Monomer of an enzyme: Amino acids are the monomers that make up enzymes (proteins).

  2. How a substrate binds: Substrates bind to an enzyme's active site, which has a specific shape complementary to the substrate.

  3. After substrate binds: The enzyme changes shape slightly (induced fit), facilitating the reaction and converting the substrate into the product.

  4. Function of an enzyme: Enzymes speed up biological reactions by lowering activation energy.

  5. True/False (Gibbs Free Energy): False – Enzymes do not affect Gibbs Free Energy; they only lower the activation energy.

  6. Enzyme's effect on reaction rate: Enzymes increase the reaction rate by providing an alternative pathway with lower activation energy.

  7. Activation energy (catalyzed vs. uncatalyzed): In an enzyme-catalyzed reaction, activation energy is lower.

  8. Reaction rate (catalyzed vs. uncatalyzed): Catalyzed reactions occur much faster than uncatalyzed ones.


Environmental Impacts on Enzymes

  1. Conditions affecting enzyme structure: Temperature and pH.

  2. Change in structure's effect: It alters the enzyme's ability to bind substrates (loss of function).

  3. Outcomes of structural change:

    • Enzyme works less effectively.

    • Enzyme stops working entirely.

    • Enzyme regains function if the change is reversible.

  4. Denaturation: Loss of an enzyme's functional shape due to environmental stress.

  5. True/False (Reversibility): True – Some enzymes can regain their structure under the right conditions.

  6. Reversible example: RNAse A.

  7. Nonreversible example: Fried egg proteins.


pH and Temperature

  1. Effect of hydrogen ions on pH:

    • Increase: pH decreases (more acidic).

    • Decrease: pH increases (more basic).

  2. Effect of pH changes on enzyme:

    • Increase: Enzyme denatures if too basic.

    • Decrease: Enzyme denatures if too acidic.

  3. Reactant concentration on rate: Higher concentrations increase reaction rate up to a saturation point.

  4. Enzyme concentration on rate: Higher enzyme levels increase reaction rate, provided substrates are available.

  5. Temperature effects:

    • Increase: Molecules move faster, but extreme heat denatures enzymes.

    • Decrease: Molecules move slower, reducing reaction rate.

  6. Temperature on molecules: Affects kinetic energy and collision frequency.


Inhibitors

  1. Competitive inhibitor: Molecule competes with the substrate for the active site.

  2. Overcoming competitive inhibitor: Increase substrate concentration.

  3. Noncompetitive inhibitor: Binds elsewhere on the enzyme, changing its shape.

  4. Inhibitor's effect on reaction rate: Slows down the reaction rate.


Energy and Thermodynamics

  1. First Law of Thermodynamics: Energy cannot be created or destroyed, only transformed.

  2. Second Law of Thermodynamics: Energy transfers increase the universe's entropy.

  3. Maintaining order: Requires energy input.

  4. Powering cellular processes: ATP (adenosine triphosphate).

  5. Endergonic reaction: Absorbs energy (e.g., photosynthesis).

  6. Exergonic reaction: Releases energy (e.g., cellular respiration).

  7. Energy coupling: Uses energy from exergonic reactions to power endergonic reactions.


Photosynthesis

  1. Energy source: Light.

  2. First photosynthetic organism: Cyanobacteria.

  3. Oxygenation evidence: Banded iron formations in ancient rocks.

  4. Light-dependent reactions: Convert light energy to ATP and NADPH.

  5. Location: Thylakoid membranes of chloroplasts.

  6. ATP synthesis: Proton gradient powers ATP synthase.

  7. NADPH synthesis: Light excites electrons, which reduce NADP+ to NADPH.

  8. Chlorophyll: Pigment capturing light energy.

  9. Photosystem and electron transport chain: Photosystem absorbs light, exciting electrons that move through the ETC.


Cellular Respiration

  1. Processes: Glycolysis, Citric Acid Cycle (Krebs), Electron Transport Chain.

  2. Products: ATP, CO₂, and water.

  3. Electron transport chain (ETC): Series of proteins transferring electrons to create a proton gradient.

  4. ETC locations:

    • Mitochondrial inner membrane (eukaryotes).

    • Plasma membrane (prokaryotes).

  5. Pathway of electrons:

    • Start: Glucose.

    • Carriers: NADH and FADH₂.

    • End: Oxygen (final acceptor).

  6. Proton gradient generation: From ETC using energy from electrons.

  7. Proton direction (ETC): Pumped from matrix to intermembrane space (mitochondria).

  8. Chemiosmosis: Proton flow through ATP synthase drives ATP production.

  9. Oxidative phosphorylation: ATP synthesis using oxygen and ETC.

  10. Photophosphorylation: ATP synthesis in photosynthesis using light energy.


Organismal Fitness

  1. Endotherm: Maintains body temperature through internal mechanisms (e.g., metabolism).

  2. Decoupling oxidative phosphorylation: Generates heat by uncoupling proton gradient from ATP synthesis.


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