AP Biology · Unit 3 · 12–16% of Exam ⚡ SPRINT MODE

Cellular Energetics

The highest-weighted unit on the entire exam. Every single topic here is ★★★. Master enzyme inhibition graphs, chemiosmosis, the 4-stage respiration table, and photosynthesis I/O cold — these are pure, predictable points.

Exam Weight12–16%
~MCQs7–10 questions
FRQ AppearanceAlmost Every Year
Sprint Time~2.5 hours
Activation EnergyInhibition GraphsOIL RIG ChemiosmosisLight ReactionsCalvin Cycle Glycolysis → ETCFermentation
⚡ Quick Glance — All Topics at a Glance
TopicPriorityExam FormatKey Trap / Must-Know
3.1 Enzymes★★★MCQDataEnzymes lower Ea only — ΔG and equilibrium UNCHANGED
3.2 Enzyme Regulation★★★MCQDataFRQCompetitive: ↑Km, same Vmax. Noncompetitive: same Km, ↓Vmax
3.3 ATP & Redox★★★MCQFRQOIL RIG; NADH/FADH₂ carry electrons TO ETC — not ATP
3.4 Photosynthesis★★★MCQFRQDataO₂ from H₂O (NOT CO₂); Calvin cycle needs light products (not truly "dark")
3.5 Cellular Respiration★★★MCQFRQData~90% ATP from ETC (not glycolysis); fermentation = NAD⁺ regeneration only
⚠ AP EXAM EXCLUSION — Do NOT memorize: specific glycolysis intermediate names, Krebs cycle intermediate names, exact ATP counts per step, or structural formulas. Know CONCEPTS, LOCATIONS, INPUTS/OUTPUTS, and relative ATP yield.
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Topic 3.1

Enzymes

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Core Definition
⚗️ What Enzymes Do (and Don't)
  • Biological catalysts — speed up reactions; not consumed
  • Lower activation energy (Ea) — energy to reach transition state
  • Do NOT change ΔG (overall free energy difference reactants → products)
  • Do NOT change equilibrium — only reach it faster
  • Do NOT make unfavorable reactions favorable
  • Reusable; specific to one substrate/reaction type
Binding Models
🤝 Induced Fit (Current Model)
  • Lock-and-Key: rigid active site; overly simplistic; NOT the preferred model
  • Induced Fit: active site is flexible; changes shape when substrate binds → forms tighter enzyme–substrate complex → AP prefers this
  • Active site = specific region where substrate binds
  • Enzyme–substrate complex (ES complex) → product released → enzyme recycled
Special Cases
🔩 Cofactors, Coenzymes & Ribozymes
  • Cofactors: inorganic ions required by enzyme (Mg²⁺, Zn²⁺, Fe²⁺)
  • Coenzymes: organic helpers (NAD⁺, FAD, Coenzyme A)
  • Ribozymes: RNA molecules that catalyze reactions — ribosomal rRNA catalyzes peptide bond formation (evidence for RNA world hypothesis)
  • Most enzymes are proteins, but not all
🎯 Exam Sniper
  • Energy diagram MCQ (very common): Given a graph of reaction progress vs. free energy — with and without enzyme — identify: (1) Ea with/without enzyme, (2) ΔG of the reaction (same both curves), (3) which curve represents the enzyme-catalyzed reaction (lower peak)
  • MCQ trap: "The enzyme makes the reaction more thermodynamically favorable." → FALSE. Enzyme only lowers Ea peak, not ΔG endpoints
  • MCQ: "Which of the following is an example of a ribozyme?" → rRNA in the ribosome (catalyzes peptide bond formation) — connects to RNA world hypothesis and evolution
  • FRQ connection: Induced fit explains why inhibitors that bind the active site (competitive) or allosteric site (noncompetitive) affect enzyme function by altering the shape
💣 Trap Alert
  • ❌ Enzymes do NOT change ΔG — the difference in free energy between reactants and products is unchanged. Enzymes only lower the hill (Ea), not the start or end points
  • ❌ Enzymes do NOT shift equilibrium — reactions still reach the same equilibrium; enzymes just get there faster
  • ❌ The induced-fit model is the AP-preferred model, not lock-and-key. Active sites are flexible and undergo conformational changes upon substrate binding
Topic 3.2

Enzyme Regulation & Environmental Impacts

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Competitive vs. Noncompetitive Inhibition — Graph Critical

🔵 Competitive Inhibition
  • Inhibitor binds active site (mimics substrate)
  • Competes directly with substrate for active site
  • Can be overcome by ↑ substrate concentration
  • Km ↑ (apparent — need more substrate for same rate)
  • Vmax unchanged (can still reach max with enough substrate)
  • Graph: same Vmax, curve shifted right
  • Example: drugs that mimic substrate (e.g., ACE inhibitors)
🔴 Noncompetitive Inhibition
  • Inhibitor binds allosteric site (not active site)
  • Changes enzyme shape → active site distorted
  • Adding more substrate does NOT overcome it
  • Km unchanged (affinity for substrate same)
  • Vmax ↓ (even saturating enzyme can't reach original Vmax)
  • Graph: lower Vmax, same Km (same curve shape, lower plateau)
  • Example: allosteric inhibitors; heavy metal poisoning (Pb²⁺, Hg²⁺)
Environmental Effects
🌡 Temperature & pH
  • Optimal temperature: fastest rate; above optimal → denaturation → loss of function (irreversible)
  • Optimal pH: each enzyme has a specific pH optimum (pepsin pH 2 in stomach; trypsin pH 8 in small intestine)
  • Above/below optimum: H-bonds, ionic bonds in enzyme broken → active site changes shape → substrate can't bind
  • Low temperature: slows reaction but does NOT denature enzyme (reversible when warmed)
Metabolic Control
🔄 Allosteric Regulation & Feedback Inhibition
  • Allosteric regulation: molecule binds site OTHER than active site → conformational change → activates or inhibits enzyme
  • Feedback inhibition: end product of a pathway inhibits an enzyme earlier in the same pathway → prevents overproduction; saves energy
  • Example: ATP inhibits phosphofructokinase (PFK) in glycolysis when energy is abundant
  • Allosteric activators: increase enzyme activity by stabilizing active conformation
🎯 Exam Sniper
  • Data Graph MCQ (top hit): Given a rate vs. [substrate] graph with and without inhibitor — if Vmax is same but curves shifts right → competitive inhibition; if Vmax is lower with parallel curve → noncompetitive inhibition
  • FRQ: "An inhibitor reduces enzyme activity even when substrate concentration is very high. Identify the type of inhibition and explain." → Noncompetitive — binds allosteric site → structural change → active site distorted → adding substrate can't help since inhibitor is at a different site
  • MCQ: "A metabolic pathway produces amino acid X. When X concentration is high, it inhibits the first enzyme in the pathway. This is an example of..." → Feedback (negative) inhibition / allosteric inhibition
  • MCQ: "An enzyme's activity drops sharply above 45°C. Which protein property explains this?" → Denaturation — hydrogen bonds and other non-covalent bonds maintaining 3° structure are disrupted → active site loses shape
Graph MCQTopic 3.2VERY HIGH FREQUENCY

An experiment measures the rate of an enzyme-catalyzed reaction at increasing substrate concentrations, with and without an inhibitor. With inhibitor present, the maximum reaction rate (Vmax) is unchanged, but the substrate concentration needed to reach half-maximal rate (Km) is doubled. What type of inhibition is this, and how does the inhibitor work?

  • (A) Noncompetitive inhibition — the inhibitor binds the active site and cannot be displaced by substrate
  • (B) Competitive inhibition — the inhibitor binds the active site and competes with substrate; adding more substrate eventually displaces it
  • (C) Allosteric inhibition — the inhibitor lowers Vmax by distorting the active site through a remote binding site
  • (D) Feedback inhibition — the inhibitor is the end product and reduces enzyme synthesis
Answer: (B) — The key clues are: Vmax unchanged + Km increased. This is the signature of competitive inhibition. The inhibitor mimics the substrate and occupies the active site, making it harder for substrate to bind (↑ apparent Km). However, because the inhibitor can be displaced by excess substrate (it's reversible), adding more substrate allows the enzyme to eventually reach the same Vmax. If Vmax had decreased, that would indicate noncompetitive inhibition.
Topic 3.3

Cellular Energy — ATP, Thermodynamics & Redox

★★★ HIGH PRIORITYMCQFRQ
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Energy Currency
⚡ ATP — The Universal Currency
  • ATP = adenosine triphosphate = adenine + ribose + 3 phosphate groups (a nucleotide!)
  • Hydrolysis: ATP → ADP + Pᵢ + energy (exergonic; ~7.3 kcal/mol released)
  • Synthesis: ADP + Pᵢ + energy → ATP (endergonic; phosphorylation)
  • ATP is not long-term storage — recharged continuously (muscle cell turns over ATP in seconds)
  • Three types of work: mechanical (muscle), transport (pumps), chemical (biosynthesis)
Thermodynamics
🔥 ΔG — Free Energy
  • Exergonic (ΔG < 0): releases free energy; spontaneous; products have less energy than reactants → cellular respiration, ATP hydrolysis
  • Endergonic (ΔG > 0): requires energy input; not spontaneous → photosynthesis, ATP synthesis, biosynthesis
  • Energy coupling: exergonic reaction (ATP hydrolysis) drives endergonic reactions
  • Enzymes lower Ea but do NOT change ΔG
Must Memorize
🔋 OIL RIG — Redox Reactions
  • OIL RIG: Oxidation Is electron Loss; Reduction Is electron Gain
  • Oxidation: lose electrons → lose H⁺ too (in biological systems) → NAD⁺ oxidizes glucose
  • Reduction: gain electrons → gain H⁺ → NAD⁺ is reduced to NADH
  • Oxidizing agent: causes oxidation (is itself reduced) → NAD⁺, FAD, O₂
  • Reducing agent: causes reduction (is itself oxidized) → glucose, NADH
  • Glucose is oxidized in respiration; CO₂ is reduced in photosynthesis
Electron Carriers
📦 NADH & FADH₂
  • NAD⁺: oxidized form (empty); accepts 2 electrons + H⁺ → becomes NADH (reduced, full)
  • FAD: oxidized form; accepts 2 electrons → becomes FADH₂
  • NADH and FADH₂ carry electrons to the electron transport chain (ETC)
  • ETC uses electron energy to pump H⁺ → drives ATP synthase
  • NADH yields ~2.5 ATP; FADH₂ yields ~1.5 ATP at the ETC
  • In photosynthesis: NADP⁺ → NADPH (similar role, different carrier)
🎯 Exam Sniper
  • MCQ: "In cellular respiration, glucose is _____ and oxygen is _____." → Glucose is oxidized (loses electrons); O₂ is reduced (gains electrons → becomes H₂O)
  • MCQ: "Which of the following is an endergonic reaction?" → Photosynthesis; ATP synthesis; protein synthesis. (NOT ATP hydrolysis or cellular respiration)
  • MCQ: "NADH functions in cellular respiration primarily by..." → Carrying electrons (and their energy) to the electron transport chain, where they are used to pump protons and generate ATP
Topic 3.4

Photosynthesis

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Overall Equation
6CO₂ + 6H₂O
+ Light →
C₆H₁₂O₆ + 6O₂

Stage-by-Stage Breakdown — Master This Table

StageLocationInputsOutputsKey Point
Light Reactions
(also: "Light-Dependent")
Thylakoid membrane (in grana) Light energy, H₂O, ADP+Pᵢ, NADP⁺ ATP, NADPH, O₂ Water is split (photolysis) → releases O₂; PS II → PS I → NADPH; ATP via chemiosmosis
Calvin Cycle
(also: "Carbon Fixation")
Stroma of chloroplast CO₂, ATP, NADPH G3P (→ used to build glucose), ADP+Pᵢ, NADP⁺ Fixes carbon (CO₂ → organic); uses ATP + NADPH from light reactions; enzyme = RuBisCO
Light Reactions — Critical Details
☀️ What Happens at the Thylakoid
  • Photosystem II (PS II): absorbs light → energizes electrons → water split (H₂O → O₂ + 2H⁺ + 2e⁻)
  • Electrons travel down ETC → H⁺ pumped into thylakoid lumen (high H⁺ inside)
  • Photosystem I (PS I): re-energizes electrons with more light → electrons used to reduce NADP⁺ → NADPH
  • H⁺ flows back through ATP synthase → ATP synthesized (chemiosmosis)
  • O₂ comes from H₂O, NOT CO₂ — proven by ¹⁸O isotope experiments
Calvin Cycle — Critical Details
🌿 What Happens in the Stroma
  • CO₂ is fixed (attached to organic molecule) by enzyme RuBisCO
  • 3 CO₂ + 3 RuBP → 6 3-carbon molecules → reduced to G3P (glyceraldehyde-3-phosphate)
  • G3P used to build glucose, amino acids, fatty acids
  • Some G3P regenerates RuBP (must keep cycle running)
  • "Light-independent" is misleading — Calvin cycle needs ATP + NADPH from light reactions. It STOPS in darkness when these run out
  • 3 turns of cycle fix 3 CO₂ → 1 net G3P (one "half" of glucose)

Chemiosmosis in Chloroplasts — The ATP Engine

Chemiosmosis — Same Mechanism in Both Photosynthesis and Respiration
☀️ In Chloroplasts (Thylakoid)
  • ETC pumps H⁺ INTO thylakoid lumen (from stroma)
  • High H⁺ inside thylakoid → concentration gradient
  • H⁺ flows OUT through ATP synthase (in thylakoid membrane) → synthesizes ATP in stroma
  • ATP + NADPH used by Calvin cycle
🔥 In Mitochondria (inner membrane)
  • ETC pumps H⁺ INTO intermembrane space (from matrix)
  • High H⁺ in IMS → concentration gradient
  • H⁺ flows BACK through ATP synthase (in inner membrane) → synthesizes ATP in matrix
  • O₂ is terminal electron acceptor → H₂O formed
🎯 Exam Sniper
  • MCQ (top hit): "What is the source of the oxygen released during photosynthesis?" → Water (H₂O) — split by PS II during the light reactions. NOT CO₂. CO₂ is fixed into carbohydrates
  • FRQ: "Explain why the Calvin cycle slows down if a plant is moved from light to dark." → Light reactions stop → ATP and NADPH not produced → Calvin cycle has no reactants → carbon fixation halts. The Calvin cycle is light-independent in mechanism but light-dependent for its substrates
  • Data Analysis: Experiments measuring O₂ production at different light intensities, CO₂ levels, or temperatures — know that increasing light, CO₂, temperature (up to optimum), and water all increase photosynthesis rate
  • MCQ: "Where does the Calvin cycle occur?" → Stroma of the chloroplast (NOT thylakoid membrane)
  • FRQ: "Describe the role of ATP synthase in photosynthesis" → Catalyzes ATP synthesis as H⁺ flows down electrochemical gradient from thylakoid lumen to stroma; same principle as in mitochondria
💣 Trap Alert
  • O₂ comes from H₂O, NOT CO₂ — this is one of the most common wrong answers on the AP exam. The oxygen in CO₂ ends up in carbohydrate (G3P/glucose)
  • Calvin cycle is NOT a "dark reaction" — it needs ATP and NADPH from light reactions. If there's no light, no ATP/NADPH, so the Calvin cycle stops within minutes
  • Plants do cellular respiration too — in mitochondria, 24 hours a day. At night, only respiration. During bright daylight, photosynthesis rate > respiration rate
  • ❌ PS II comes BEFORE PS I in the light reactions (numbered by discovery order, not pathway order)
Topic 3.5

Cellular Respiration

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Overall Equation — Aerobic Respiration
C₆H₁₂O₆ + 6O₂
6CO₂ + 6H₂O + ~30–32 ATP

The 4 Stages — Master This Table

StageLocationO₂ Needed?InputsDirect OutputsNet ATP
1. Glycolysis Cytosol ❌ No Glucose (1) 2 pyruvate, 2 NADH, 2 ATP net 2 ATP
2. Pyruvate Oxidation
(pyruvate → acetyl-CoA)
Mitochondrial matrix ✅ Yes (O₂ indirectly) 2 pyruvate, CoA, NAD⁺ 2 acetyl-CoA, 2 NADH, 2 CO₂ 0 ATP
3. Krebs Cycle
(Citric acid cycle)
Mitochondrial matrix ✅ Yes (indirectly) 2 acetyl-CoA, H₂O, NAD⁺, FAD 6 NADH, 2 FADH₂, 2 ATP, 4 CO₂ 2 ATP
4. Oxidative Phosphorylation
(ETC + ATP synthase)
Inner mitochondrial membrane ✅ Yes — O₂ is terminal e⁻ acceptor 10 NADH, 2 FADH₂, O₂ ~26–28 ATP, H₂O ~26–28 ATP
Critical Concept
⚙️ Where Does ATP Actually Come From?
  • Glycolysis + Krebs: only 4 ATP total (substrate-level phosphorylation)
  • NADH + FADH₂ carry electrons to ETC → produce ~26–28 ATP (oxidative phosphorylation)
  • ~90% of ATP from ETC/oxidative phosphorylation
  • H⁺ gradient (from ETC pumping) drives ATP synthase — chemiosmosis
  • NADH yields ~2.5 ATP; FADH₂ yields ~1.5 ATP (enters ETC lower down)
  • O₂ accepts electrons at the end → forms H₂O
Without Oxygen
🍺 Fermentation — The Backup Plan
  • Occurs when O₂ is absent (anaerobic conditions)
  • Glycolysis still runs → produces 2 ATP + 2 NADH + 2 pyruvate
  • Fermentation's ONLY purpose: regenerate NAD⁺ from NADH so glycolysis can continue
  • NO additional ATP produced in fermentation steps themselves
  • Two types: Lactic acid fermentation (animals, some bacteria: pyruvate → lactate + NAD⁺); Alcoholic fermentation (yeast: pyruvate → ethanol + CO₂ + NAD⁺)
  • Total ATP = only 2 ATP (from glycolysis)
Where CO₂ is Released
💨 Tracking Carbon
  • Glycolysis: NO CO₂ released (glucose → pyruvate, all C retained)
  • Pyruvate oxidation: 2 CO₂ released (one per pyruvate)
  • Krebs cycle: 4 CO₂ released (two per acetyl-CoA × 2 turns)
  • ETC/chemiosmosis: NO CO₂ released
  • Total: 6 CO₂ from 1 glucose (matches overall equation)
  • All carbon from glucose ends up as CO₂ by end of Krebs
🎯 Exam Sniper
  • FRQ (most common Unit 3 FRQ): Describe the role of the electron transport chain in ATP synthesis → Electrons from NADH and FADH₂ pass through protein complexes in inner mitochondrial membrane → energy used to pump H⁺ from matrix to intermembrane space → H⁺ gradient drives H⁺ back through ATP synthase → conformational change in synthase → ADP + Pᵢ → ATP. O₂ accepts electrons at end → H₂O
  • MCQ: "If a cell's mitochondria are destroyed, which ATP-producing process can still occur?" → Glycolysis (occurs in cytosol, no mitochondria needed)
  • MCQ: "Why does yeast produce ethanol during fermentation?" → To regenerate NAD⁺ from NADH — NAD⁺ is needed to keep glycolysis running (as an electron acceptor)
  • Data Analysis: Graph of CO₂ production in yeast — under anaerobic conditions: slow CO₂ (from fermentation); aerobic: more CO₂ (from respiration) — explains why winemaking uses anaerobic conditions
  • MCQ: "A drug blocks ATP synthase. Which stage of respiration is most directly affected?" → Oxidative phosphorylation — ETC still runs but H⁺ can't drive ATP synthesis. Result: H⁺ gradient builds up, ETC eventually stops too
💣 Trap Alert
  • ~90% of ATP from oxidative phosphorylation (ETC), NOT glycolysis or Krebs. Glycolysis = 2 ATP, Krebs = 2 ATP, ETC = ~26–28 ATP
  • Fermentation produces NO extra ATP — its only role is regenerating NAD⁺ so glycolysis can continue. Total ATP from fermentation = 2 (from glycolysis only)
  • Glycolysis happens in the CYTOSOL, not the mitochondria. Prokaryotes can do glycolysis (no mitochondria)
  • O₂ is the terminal electron acceptor, not the source of energy directly. O₂ pulls electrons down the ETC, allowing H⁺ to be pumped. It becomes H₂O at the end
  • ❌ CO₂ is produced in pyruvate oxidation AND Krebs cycle — NOT in glycolysis or the ETC
FRQ-Style MCQTopic 3.5HIGHEST FREQUENCY

A researcher adds a chemical that makes the inner mitochondrial membrane permeable to H⁺ ions (a "proton uncoupler"). Which of the following best describes the effect on cellular respiration?

  • (A) Glycolysis would stop because glucose can no longer be phosphorylated
  • (B) The Krebs cycle would stop because acetyl-CoA cannot enter the matrix
  • (C) The ETC would continue but ATP synthesis would decrease because the H⁺ gradient collapses
  • (D) Oxygen consumption would decrease because the ETC no longer has electrons to transfer
Answer: (C) — ATP synthesis via chemiosmosis depends on the H⁺ concentration gradient across the inner mitochondrial membrane. A proton uncoupler dissipates this gradient by allowing H⁺ to leak back freely without going through ATP synthase. Result: the ETC still accepts electrons (NADH, FADH₂ still donate electrons; O₂ still accepts them → O₂ consumption may even INCREASE), but the H⁺ energy is released as heat rather than captured as ATP. This is why some uncouplers (like DNP) cause hyperthermia — the energy becomes heat. ATP production crashes.
Practice

Sprint Practice — Mixed Questions

Cross-Topic MCQPhotosynthesis + Respiration

A plant is kept in a sealed container in bright light. Initially, CO₂ decreases and O₂ increases. After several hours, gas concentrations stabilize with no further net change. Which explanation best accounts for the stabilization?

  • (A) The plant ran out of chlorophyll and can no longer photosynthesize
  • (B) Photosynthesis rate equals cellular respiration rate, so net O₂ and CO₂ exchange is zero
  • (C) The Calvin cycle stopped because there is no CO₂ left to fix
  • (D) The plant switched entirely to anaerobic fermentation
Answer: (B) — Plants carry out BOTH photosynthesis (consumes CO₂, produces O₂) and cellular respiration (consumes O₂, produces CO₂) simultaneously. As CO₂ is depleted and O₂ builds up, photosynthesis rate decreases (less substrate) while CO₂ from respiration is recycled into the system. Equilibrium is reached when the two rates are equal — this is called the compensation point. The plant is still metabolically very active; it's just that the inputs and outputs cancel each other out.
Data AnalysisEnzyme Inhibition

The following data were collected for an enzyme at varying substrate concentrations:

Without inhibitor: Vmax = 100 μmol/min, Km = 4 mM
With inhibitor X: Vmax = 100 μmol/min, Km = 12 mM
With inhibitor Y: Vmax = 50 μmol/min, Km = 4 mM

What are the types of inhibitors X and Y, and what do the results tell us about each mechanism?

  • (A) X = noncompetitive; Y = competitive
  • (B) X = competitive; Y = noncompetitive
  • (C) Both X and Y are competitive inhibitors
  • (D) X = allosteric activator; Y = feedback inhibitor
Answer: (B) — Inhibitor X: Vmax unchanged (100) but Km tripled (4 → 12 mM) → classic signature of competitive inhibition. The inhibitor competes for the active site; adding more substrate can displace it, so Vmax is still reachable. Inhibitor Y: Km unchanged (4 mM, same affinity for substrate) but Vmax halved (100 → 50) → classic noncompetitive inhibition. Binds allosteric site → distorts active site → even saturating substrate can't restore original Vmax. This data-reading skill is tested almost every year.
FRQ-StylePhotosynthesis Mechanism

A scientist treats isolated chloroplasts with a drug that blocks Photosystem II but leaves Photosystem I functional. Predict what happens to: (A) O₂ production, (B) NADPH production, and (C) ATP synthesis in the Calvin cycle.

  • (A) O₂ decreases; NADPH increases; Calvin cycle ATP synthesis increases
  • (B) O₂ production stops; NADPH production stops; Calvin cycle cannot proceed
  • (C) O₂ production stops; NADPH production continues normally; Calvin cycle is unaffected
  • (D) All three processes decrease proportionally but do not stop
Answer: (B) — PS II is blocked: (A) No water splitting → NO O₂ produced. (B) PS II feeds electrons into the ETC → PS I. If PS II is blocked, no electrons flow to PS I → PS I cannot reduce NADP⁺ → NO NADPH. (C) Without ATP (from ETC/chemiosmosis, which also requires electron flow from PS II) and NADPH, the Calvin cycle has no substrates → cannot fix CO₂. The entire photosynthetic system collapses from the blockage of PS II — it is the gateway of the light reactions.
⚠ Trap Alert

Unit 3 High-Frequency Exam Traps

✓ Last-Min Checklist

Pre-Exam 10-Minute Checklist

Click each item to check off before exam day.

Enzymes & Regulation (3.1–3.2)

ATP & Redox (3.3)

Photosynthesis (3.4)

Cellular Respiration (3.5)

⚡ Final Sprint Strategy for Unit 3
  • Top 5 must-master concepts: (1) Inhibition graph reading (Km/Vmax changes), (2) Photosynthesis stage I/O table + O₂ from H₂O, (3) Respiration 4-stage location/I/O table, (4) Chemiosmosis mechanism (applies to BOTH organelles), (5) Fermentation = NAD⁺ only, no extra ATP
  • FRQ templates to know: "Trace electrons from glucose to ATP synthesis" (respiration ETC); "Explain why plants need both light and dark conditions for photosynthesis"; "Compare competitive and noncompetitive inhibition using a graph"
  • The AP CED explicitly excludes: intermediate names in glycolysis (glucose-6-phosphate, etc.), specific Krebs intermediates (citrate, oxaloacetate, etc.), precise ATP counts per step. Focus on relative amounts and conceptual understanding
  • Connections: Unit 1 (ATP = nucleotide derivative); Unit 2 (chemiosmosis uses membrane gradient like active transport); Unit 4 (ATP hydrolysis powers signal transduction); Unit 5 (enzymes used in DNA replication = same principles)
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