Question 1

Key features of oxidative phosphorylation Which statement describes something that is not a feature of oxidative phosphorylation in mitochondria?

Accepted Answer

Introduction / Context: There are two fundamental modes of ATP formation: substrate-level phosphorylation and oxidative phosphorylation. Distinguishing these mechanisms is essential for mapping where ATP arises in metabolism. Given Data / Assumptions: Oxidative phosphorylation occurs in mitochondria using electron transport to build PMF. ATP synthase (Complex V) uses PMF to synthesize ATP. Substrate-level phosphorylation transfers phosphate directly from an intermediate to ADP (e.g., in glycolysis and TCA at succinyl-CoA synthetase). Concept / Approach: Oxidative phosphorylation relies on proton pumping by respiratory complexes I, III, and IV, generating ΔΨ and ΔpH. ATP synthase then catalyzes ADP + Pi → ATP using this PMF. No direct high-energy phosphate transfer from a metabolic intermediate to ADP occurs in this process. Step-by-Step Solution: Identify the defining feature: chemiosmotic coupling to ATP synthase.Note that substrate-level ATP formation is separate and occurs in cytosol/mitochondrial matrix at specific enzymes.Conclude that direct phosphate transfer is not a feature of oxidative phosphorylation. Verification / Alternative check: Inhibitors/uncouplers (oligomycin, FCCP) that affect PMF or ATP synthase specifically reduce oxidative phosphorylation but not substrate-level phosphorylation steps, underscoring their mechanistic differences. Why Other Options Are Wrong: Electrochemical gradient, ATP synthase, protonmotive force, and coupling to electron transport are all core features of oxidative phosphorylation. Common Pitfalls: Confusing succinyl-CoA synthetase (substrate-level phosphorylation) with ATP synthase; assuming all mitochondrial ATP arises from the same mechanism. Final Answer: Direct transfer of phosphate from a substrate molecule to ADP.

Question 2

Entry of glycolytic products into mitochondria In aerobic respiration, which compound produced in the cytosol typically enters the mitochondrion before being converted to acetyl-CoA by the pyruvate dehydrogenase complex?

Accepted Answer

Introduction / Context: Linking glycolysis to the citric acid cycle requires transport of carbon from the cytosol into mitochondria. Identifying which metabolite crosses the mitochondrial membranes clarifies the organization of central metabolism. Given Data / Assumptions: Glycolysis occurs in the cytosol and produces pyruvate. Pyruvate is transported into the mitochondrial matrix by the mitochondrial pyruvate carrier. Inside the matrix, pyruvate dehydrogenase converts pyruvate to acetyl-CoA, CO2, and NADH. Concept / Approach: Acetyl-CoA is generated inside mitochondria; it does not cross the inner membrane efficiently. Therefore, the transported species is pyruvate, not acetyl-CoA. Other glycolytic intermediates, like glyceraldehyde-3-phosphate (phosphoglyceraldehyde), remain in the cytosol during glycolysis. Step-by-Step Solution: Cytosolic glycolysis ends with pyruvate formation.Pyruvate crosses the inner membrane via the pyruvate carrier.Matrix conversion: pyruvate + CoA + NAD+ → acetyl-CoA + CO2 + NADH. Verification / Alternative check: Tracer studies show rapid mitochondrial uptake of pyruvate; acetyl-CoA accumulation requires intact pyruvate dehydrogenase, supporting intra-mitochondrial generation. Why Other Options Are Wrong: Acetyl-CoA: generally cannot exit/enter across the inner membrane; it is formed inside.Phosphoglyceraldehyde: remains a cytosolic glycolytic intermediate.Oxaloacetate has limited permeability and is typically generated inside depending on shuttles.Lactate is converted to pyruvate (via LDH) before mitochondrial oxidation in most tissues. Common Pitfalls: Assuming acetyl-CoA is transported directly; overlooking the dedicated pyruvate carrier. Final Answer: Pyruvate.

Question 3

Cellular respiration stoichiometry: For complete aerobic oxidation of carbohydrate, how many molecules of CO2 are exhaled for each molecule of O2 consumed (i.e., the respiratory quotient for carbohydrates)?

Accepted Answer

Introduction / Context: The respiratory quotient (RQ) links gas exchange to metabolism. For substrates like glucose oxidized aerobically, RQ helps quantify how many carbon dioxide molecules are produced per oxygen molecule consumed, a classic physiology and biochemistry concept. Given Data / Assumptions: Aerobic, steady-state oxidation of a carbohydrate such as glucose. Complete oxidation: glucose + O2 → CO2 + H2O with ATP production. No contribution from fats or proteins (which have different RQ values). Concept / Approach: For glucose, the balanced reaction is commonly written as: C6H12O6 + 6 O2 → 6 CO2 + 6 H2O. RQ is defined as CO2 produced / O2 consumed. For pure carbohydrate, this ratio equals 1. This reflects the matching of carbon oxidation to oxygen reduction when the substrate has an average oxidation state compatible with complete combustion to CO2 and H2O. Step-by-Step Solution: Write the overall equation: C6H12O6 + 6 O2 → 6 CO2 + 6 H2O.Compute the ratio: CO2 produced / O2 consumed = 6 / 6.Simplify the ratio to 1 CO2 per 1 O2.Therefore, for each O2, one CO2 is exhaled on average during carbohydrate oxidation. Verification / Alternative check: Indirect calorimetry in exercise physiology routinely measures RQ ≈ 1.0 for pure carbohydrate metabolism, confirming the stoichiometric calculation. Why Other Options Are Wrong: 3, 6, 12: These do not reflect the standard molar ratio and would imply non-physiologic stoichiometry for carbohydrate. Common Pitfalls: Confusing mixed-fuel oxidation (fats have RQ ≈ 0.7; proteins ≈ 0.8–0.9) with pure carbohydrate; always specify the substrate when interpreting RQ. Final Answer: 1

Question 4

In mitochondrial electron transport, what is the role of Coenzyme Q (ubiquinone)?

Accepted Answer

Introduction / Context: Coenzyme Q (ubiquinone, abbreviated Q or CoQ10) is central to the mitochondrial electron transport chain (ETC). Understanding its physical nature and position clarifies how electrons and protons move across the inner mitochondrial membrane to drive ATP synthesis. Given Data / Assumptions: Oxidative phosphorylation in eukaryotic mitochondria. Complex I and II feed electrons to Q; Complex III receives electrons from reduced Q (QH2). Inner mitochondrial membrane is hydrophobic. Concept / Approach: Ubiquinone is a small, isoprenoid-derived, lipid-soluble benzoquinone. Because it dissolves in the inner membrane lipid bilayer, it can freely diffuse laterally to shuttle electrons from membrane-bound dehydrogenases (Complex I/II) to Complex III. It is not the terminal acceptor (that is O2 at Complex IV), nor is it a water-soluble carrier. Step-by-Step Solution: Identify CoQ's chemical character: hydrophobic tail → membrane solubility.Trace electron path: NADH/FADH2 → Complex I/II → Q → Complex III.Conclude its role: a lipid-soluble electron carrier within the membrane. Verification / Alternative check: Spectral and inhibitor studies (e.g., antimycin A on Complex III) support Q’s mobile carrier role distinct from protein-bound cytochromes. Why Other Options Are Wrong: Direct electron transfer to O2: done by Complex IV, not Q. Water-soluble donor: Q is not water-soluble; cytochrome c is water-soluble but peripherally associated. Covalent cytochrome cofactor: Q is not covalently bound to cytochromes. Common Pitfalls: Confusing Q with cytochrome c; the latter is water-soluble in the intermembrane space, whereas Q is membrane-soluble. Final Answer: A lipid-soluble electron carrier

Question 5

Fundamentals of redox chemistry: A biological oxidation–reduction (redox) reaction always involves which of the following components or events?

Accepted Answer

Introduction / Context: Redox reactions are the backbone of cellular energy conversion, from glycolysis and the Krebs cycle to the electron transport chain. Recognizing what must be present in any redox process is foundational for biochemistry and physiology. Given Data / Assumptions: Redox implies electron transfer between chemical species. Oxidation is electron loss; reduction is electron gain. Agents are named by the process they cause in others. Concept / Approach: In every redox pair, one species (reducing agent) donates electrons and becomes oxidized, while the other (oxidizing agent) accepts electrons and becomes reduced. Thus, there is always a gain of electrons by one partner and a loss by the other, occurring simultaneously. Step-by-Step Solution: Define oxidation: loss of electrons; define reduction: gain of electrons.Identify agents: reducing agent donates; oxidizing agent accepts.Conclude: any redox reaction includes an oxidizing agent, a reducing agent, and a gain of electrons by the reduced partner. Verification / Alternative check: Half-reaction notation always pairs an oxidation half-reaction with a reduction half-reaction, confirming the required components. Why Other Options Are Wrong: Listing any single element (A, B, or C) is incomplete; all are simultaneously true in a redox event. Common Pitfalls: Confusing the direction of electron flow or mislabeling agents; remember the mnemonic “OIL RIG”: Oxidation Is Loss, Reduction Is Gain. Final Answer: All of these

Question 6

Muscle metabolism during intense exercise: Lactic acid accumulates primarily because of a lack of which critical factor?

Accepted Answer

Introduction / Context: During strenuous exercise, oxygen delivery can lag behind demand in working muscle. Cells then rely more on anaerobic pathways, leading to lactate formation. Understanding the trigger for this metabolic shift is key in exercise physiology. Given Data / Assumptions: High ATP demand and limited oxygen supply in active muscle. Glycolysis continues to generate ATP rapidly. NAD+ must be regenerated to sustain glycolytic flux. Concept / Approach: When the electron transport chain slows due to insufficient O2 (the terminal electron acceptor), NADH cannot be reoxidized efficiently by oxidative phosphorylation. Cells regenerate NAD+ by reducing pyruvate to lactate via lactate dehydrogenase, enabling glycolysis to continue. Step-by-Step Solution: O2 scarcity limits electron flow at Complex IV in mitochondria.NADH oxidation slows, lowering available NAD+ for glyceraldehyde-3-phosphate dehydrogenase in glycolysis.Pyruvate is reduced to lactate, oxidizing NADH to NAD+ and sustaining ATP production.Therefore, the proximate cause for lactate accumulation is lack of oxygen. Verification / Alternative check: Measurements show increased lactate and decreased tissue O2 during peak exertion; lactate falls as O2 delivery and oxidative phosphorylation recover. Why Other Options Are Wrong: NAD+: It is regenerated by lactate formation; the initial problem is limited O2. Glucose: Typically abundant from glycogen; not the immediate limiting factor. ADP and Pi: These accumulate to stimulate respiration; they are not lacking. Common Pitfalls: Assuming lactate is simply a “waste product”; it is also a valuable fuel and signaling molecule, shuttled to liver and heart. Final Answer: Oxygen

Question 7

Pathway overview: The aerobic breakdown of glucose (cellular respiration) includes which stages?

Accepted Answer

Introduction / Context: Aerobic respiration converts the chemical energy of glucose into ATP through a coordinated series of pathways. Knowing the canonical stages helps organize a mental model for where carbon flows and where ATP and reduced cofactors are made. Given Data / Assumptions: Aerobic conditions with functional mitochondria. Glucose as the starting substrate. Standard eukaryotic pathway names applied. Concept / Approach: Cellular respiration consists of glycolysis (cytosol), pyruvate oxidation and the Krebs cycle (mitochondrial matrix), and oxidative phosphorylation (ETC and ATP synthase at the inner mitochondrial membrane). Electron transport phosphorylation uses the proton motive force to synthesize ATP. Step-by-Step Solution: Glycolysis converts glucose to pyruvate, netting ATP and NADH.Krebs cycle oxidizes acetyl-CoA to CO2, generating NADH and FADH2.Electron transport phosphorylation oxidizes NADH/FADH2 to drive ATP synthesis.All three are integral to complete aerobic glucose breakdown. Verification / Alternative check: Blockade of any stage (e.g., ETC inhibitors) reduces ATP yield dramatically, underscoring the necessity of all components in aerobic metabolism. Why Other Options Are Wrong: Each single pathway alone is insufficient; full aerobic respiration requires the entire sequence. Common Pitfalls: Overlooking pyruvate oxidation (PDH complex) as the link between glycolysis and the Krebs cycle; while not listed in the options, it is implied in the overall flow. Final Answer: All of the above

Question 8

During glycolysis, the electrons removed from glucose-derived intermediates are accepted by which cofactor?

Accepted Answer

Introduction / Context: Glycolysis harvests energy by oxidizing glucose to pyruvate. Electrons captured during this process must be accepted by an oxidized cofactor to form a reduced carrier that later yields ATP via respiration or fermentation pathways. Given Data / Assumptions: Focus on cytosolic glycolysis in most cells. Key oxidation step is catalyzed by glyceraldehyde-3-phosphate dehydrogenase. Standard cofactors NAD+/FAD are potential acceptors in metabolism. Concept / Approach: In glycolysis, glyceraldehyde-3-phosphate is oxidized and phosphorylated, and the electrons are transferred to NAD+ to form NADH. FAD is not used in the glycolytic pathway; it appears in later stages like the Krebs cycle (e.g., succinate dehydrogenase). Step-by-Step Solution: Identify the oxidation step: glyceraldehyde-3-phosphate → 1,3-bisphosphoglycerate.Note the cofactor: NAD+ accepts electrons and protons → NADH.Confirm no role for FAD, acetyl-CoA, or pyruvate as electron acceptors in glycolysis.Therefore, the correct cofactor is NAD+. Verification / Alternative check: Glycolytic stoichiometry shows a net production of 2 NADH per glucose, matching acceptance by NAD+. Why Other Options Are Wrong: FAD: used in the Krebs cycle, not glycolysis. Acetyl-CoA/Pyruvate: metabolic intermediates, not primary electron acceptors in glycolysis. Common Pitfalls: Confusing glycolytic and mitochondrial dehydrogenases; always anchor cofactors to the specific pathway step. Final Answer: NAD+

Question 9

Carbon dioxide production: In aerobic glucose catabolism, CO2 is produced primarily during which stage?

Accepted Answer

Introduction / Context: Tracking where CO2 emerges clarifies which steps fully oxidize carbon. While several stages handle electrons, only specific reactions release carbon dioxide during aerobic metabolism of glucose. Given Data / Assumptions: Glucose is fully oxidized to CO2 and H2O under aerobic conditions. Pyruvate dehydrogenase and the Krebs cycle decarboxylate carbon. ETC does not release CO2; it reduces O2 to H2O. Concept / Approach: After glycolysis generates pyruvate, pyruvate is converted to acetyl-CoA (releasing CO2). Inside the Krebs cycle, two decarboxylation steps per acetyl-CoA release two CO2. Across one glucose (two acetyl-CoA), four CO2 are produced in the Krebs cycle, with an additional two from pyruvate oxidation. Step-by-Step Solution: Glycolysis: no net CO2 release.Pyruvate → acetyl-CoA: decarboxylation releases CO2 (link step).Krebs cycle: two decarboxylations per turn produce CO2.ETC: consumes O2 to form H2O; no CO2 production. Verification / Alternative check: Textbook stoichiometry for glucose oxidation confirms CO2 generation coupled to pyruvate dehydrogenase and Krebs cycle decarboxylations. Why Other Options Are Wrong: Glycolysis: occurs in cytosol with no CO2 output. ETC: redox-driven proton pumping and water formation, not decarboxylation. Lactate fermentation: reduces pyruvate to lactate without CO2. Common Pitfalls: Overlooking the pyruvate dehydrogenase step; although not listed, the majority of CO2 per glucose is tied to mitochondrial oxidative decarboxylations. Final Answer: Krebs cycle (citric acid cycle)

Question 10

Energy currency: The complete oxidation of glucose ultimately provides usable cellular energy predominantly in the form of which molecule?

Accepted Answer

Introduction / Context: Cells convert nutrient energy into a universally useful form. While multiple reduced cofactors are produced during catabolism, the immediate “spendable” currency for biological work is ATP. Given Data / Assumptions: Glucose oxidation yields NADH and FADH2. Oxidative phosphorylation converts redox energy into ATP via ATP synthase. ATP powers transport, biosynthesis, and mechanical work. Concept / Approach: Although NADH and FADH2 carry high-energy electrons, their energy is realized as ATP through the electron transport chain and chemiosmotic phosphorylation. Coenzyme A and pyruvate are intermediates, not energy currency. Step-by-Step Solution: Glycolysis and Krebs cycle produce ATP directly (substrate-level) and NADH/FADH2.ETC uses NADH/FADH2 to pump protons, storing energy in a gradient.ATP synthase uses this gradient to form ATP from ADP + Pi.Therefore, the usable end product is ATP. Verification / Alternative check: Cellular processes universally utilize ATP hydrolysis (ATP → ADP + Pi) to drive endergonic reactions. Why Other Options Are Wrong: FADH2: carrier, not the principal energy currency. Coenzyme A/Pyruvate: metabolic intermediates. Common Pitfalls: Equating high-energy electron carriers with direct energy spend; cells must convert their energy into ATP to perform most work. Final Answer: ATP

Question 11

During which stage of aerobic glucose catabolism is FAD reduced to FADH2?

Accepted Answer

Introduction / Context: NAD+ and FAD are key oxidized cofactors that capture electrons during catabolism. Knowing where each is reduced helps map energy flow into the electron transport chain. Given Data / Assumptions: NADH is produced in multiple steps (glycolysis, PDH, Krebs). FADH2 is more restricted in its points of formation. Aerobic conditions with intact mitochondrial function. Concept / Approach: Within the Krebs cycle, succinate dehydrogenase catalyzes succinate → fumarate while reducing FAD to FADH2. This enzyme is also Complex II of the ETC, directly funneling electrons from FADH2 into the chain. Step-by-Step Solution: Identify the reaction: succinate + FAD → fumarate + FADH2.Locate it within metabolism: Krebs cycle in the mitochondrial matrix/inner membrane interface.Conclude that FADH2 formation occurs during the Krebs cycle. Verification / Alternative check: Biochemical maps consistently show FADH2 generated only at the succinate dehydrogenase step for glucose oxidation. Why Other Options Are Wrong: Electron transport: consumes NADH/FADH2, does not form them. Fermentation/Glycolysis: employ NAD+/NADH, not FAD/FADH2. Common Pitfalls: Assuming all dehydrogenations use NAD+; FAD is used when the reaction chemistry requires a stronger oxidant or involves C–C to C=C conversions. Final Answer: Krebs cycle (citric acid cycle)

Question 12

Order of pathways: Choose the correct sequence for complete aerobic oxidation of glucose in eukaryotic cells.

Accepted Answer

Introduction / Context: Pathway order determines where ATP and reducing equivalents are generated and how carbon flows to CO2. Getting the sequence right is essential for interpreting metabolic data and inhibitor effects. Given Data / Assumptions: Standard eukaryotic metabolism under aerobic conditions. Glucose is the starting substrate; oxygen is available. Pyruvate dehydrogenase links glycolysis to the Krebs cycle. Concept / Approach: Glycolysis occurs first in the cytosol, producing pyruvate (and ATP/NADH). Pyruvate is converted to acetyl-CoA, which enters the Krebs cycle in the mitochondrial matrix, generating more NADH and FADH2. Finally, the electron transport chain uses these reduced cofactors to drive ATP synthesis. Step-by-Step Solution: Start: Glycolysis (glucose → pyruvate) with substrate-level ATP production.Link: Pyruvate oxidation (PDH) forms acetyl-CoA.Next: Krebs cycle oxidizes acetyl-CoA to CO2, producing NADH/FADH2.Final: Electron transport chain harnesses NADH/FADH2 to synthesize ATP. Verification / Alternative check: Experimental inhibition (e.g., rotenone, antimycin, cyanide) stops ATP gain after NADH formation, showing ETC is downstream of glycolysis and the Krebs cycle. Why Other Options Are Wrong: Any sequence starting with Krebs or ETC ignores the need for glycolysis-derived carbon entry and reduced cofactors. Common Pitfalls: Forgetting the PDH step between glycolysis and the Krebs cycle; although not named in options, it is implied in the correct order. Final Answer: Glycolysis → Krebs cycle → Electron transport chain

Question 13

Cellular respiration — In the mitochondrial electron transport chain, which molecule serves as the final (terminal) electron acceptor?

Accepted Answer

Introduction / Context: The electron transport chain (ETC) in aerobic respiration is a series of redox carriers embedded in the inner mitochondrial membrane. Electrons flow from reduced substrates (such as NADH and FADH2) through complexes and mobile carriers to a terminal electron acceptor. Knowing the identity of this final acceptor is essential to understand how oxidative phosphorylation proceeds and why oxygen is vital for aerobic life. Given Data / Assumptions: Aerobic respiration uses oxygen and produces water. ETC components include Complex I–IV and mobile carriers (ubiquinone and cytochromes). ATP synthesis is driven by a proton motive force established by proton pumping linked to electron flow. Concept / Approach: Electrons donated by NADH and FADH2 pass sequentially to carriers of increasing reduction potential. At Complex IV (cytochrome c oxidase), electrons are finally transferred to molecular oxygen. Oxygen is reduced to water, and this step is tightly coupled to proton pumping that sustains the electrochemical gradient used by ATP synthase. Step-by-Step Solution: Electrons enter at Complex I (from NADH) or Complex II (from FADH2).They transit via ubiquinone (CoQ) to Complex III, then to cytochrome c.At Complex IV, electrons are transferred to O2, forming H2O.This terminal step allows continuous electron flow and proton pumping. Verification / Alternative check: Blocking oxygen availability (e.g., cyanide inhibition at Complex IV or anoxia) halts electron flow, collapses the proton motive force, and stops ATP synthesis—confirming oxygen's role as the terminal electron acceptor. Why Other Options Are Wrong: ADP is the substrate for ATP synthase, not an electron acceptor. Cytochrome b is an intermediate carrier within Complex III, not terminal. “None of these” is incorrect because oxygen is correct. Common Pitfalls: Confusing oxygen with water: oxygen is the acceptor; water is the reduced product. Also, mistaking cytochromes as final recipients; they are intermediates. Final Answer: Oxygen

Question 14

Mitochondrial bioenergetics — During electron transport, protons are pumped at all major sites EXCEPT which complex?

Accepted Answer

Introduction / Context: The proton motive force (PMF) that drives ATP synthesis is created by proton pumping linked to electron transfer across the inner mitochondrial membrane. Not every respiratory complex pumps protons. Identifying which complexes contribute directly to the PMF is a core concept in oxidative phosphorylation. Given Data / Assumptions: Main respiratory complexes: I (NADH dehydrogenase), II (succinate dehydrogenase), III (cytochrome bc1), IV (cytochrome c oxidase). Mobile carriers: ubiquinone (CoQ) and cytochrome c shuttle electrons. ATP synthase uses the PMF to produce ATP from ADP and Pi. Concept / Approach: Complexes I, III, and IV translocate protons from the matrix to the intermembrane space. Complex II transfers electrons from succinate to ubiquinone but does not pump protons. Thus, electron entry via FADH2 (Complex II) yields less ATP than entry via NADH (Complex I) because fewer protons are pumped per electron pair. Step-by-Step Solution: Complex I: pumps protons while moving electrons from NADH to CoQ.Complex II: accepts electrons from succinate (FADH2) to CoQ without proton pumping.Complex III: pumps protons via the Q-cycle while moving electrons to cytochrome c.Complex IV: pumps protons and reduces O2 to H2O. Verification / Alternative check: Stoichiometric models and inhibitors (rotenone, antimycin A, cyanide) demonstrate that only I, III, and IV contribute to proton pumping, matching observed ATP yields. Why Other Options Are Wrong: Complex I, III, and IV each pump protons and contribute to the PMF. Common Pitfalls: Assuming all electron-transfer steps pump protons; Complex II is an exception despite its central role in the TCA cycle and ETC. Final Answer: Complex II

Question 15

Fate of pyruvate under aerobic conditions — After glycolysis, when oxygen is available as the terminal electron acceptor, which process predominates?

Accepted Answer

Introduction / Context: Glycolysis yields pyruvate, ATP, and NADH. The cell’s next steps depend on oxygen availability. Under aerobic conditions, mitochondria oxidize reduced cofactors to drive ATP formation via oxidative phosphorylation, rather than regenerating NAD+ through fermentation. Given Data / Assumptions: Oxygen is present to act as the final electron acceptor. Glycolysis has already produced pyruvate and NADH. Choice is among processes occurring after glycolysis. Concept / Approach: With oxygen, pyruvate is converted to acetyl-CoA, enters the TCA cycle, and generates more NADH and FADH2. These reduced cofactors feed the ETC, producing a proton motive force used by ATP synthase. The defining aerobic step is oxidative phosphorylation, which captures free energy from electron transfer to synthesize ATP. Step-by-Step Solution: Glycolysis products: 2 pyruvate + 2 ATP (net) + 2 NADH per glucose.Aerobic fate: pyruvate → acetyl-CoA → TCA cycle → NADH/FADH2.ETC: electrons from NADH/FADH2 → O2, pumping protons.ATP synthesis: oxidative phosphorylation via ATP synthase. Verification / Alternative check: Measured oxygen consumption aligns with ATP yields far exceeding fermentation, confirming that oxidative phosphorylation predominates when O2 is available. Why Other Options Are Wrong: “Pyruvate is formed” and “NADH is produced” describe glycolysis itself, not what follows. Fermentation occurs when O2 is absent, to reoxidize NADH to NAD+. Common Pitfalls: Equating “aerobic” solely with the TCA cycle; the defining ATP-yielding process is oxidative phosphorylation in the mitochondrion. Final Answer: Oxidative phosphorylation

Question 16

Biological oxidants — Which of the following is NOT considered a significant biological oxidizing agent in standard metabolism?

Accepted Answer

Introduction / Context: Redox cofactors drive metabolic pathways by accepting or donating electrons. Identifying physiologically important oxidizing agents clarifies electron flow in catabolism and respiration. Given Data / Assumptions: NAD+ and FAD are classic oxidized cofactors that accept electrons. O2 is the terminal electron acceptor in aerobic respiration. Fe3+ and Fe2+ interconvert in proteins, but free ferric ion is not a common soluble oxidant in cytosolic biochemistry. Concept / Approach: In cells, NAD+ and FAD accept electrons to become NADH and FADH2, respectively. Molecular oxygen accepts electrons at Complex IV to form water. While iron cycles in heme and iron–sulfur centers, “free” Fe3+ is not broadly deployed as a primary soluble oxidant in standard metabolic reactions due to tight sequestration by proteins (to prevent radical chemistry) and limited availability. Therefore, compared with NAD+, FAD, and O2, Fe3+ is not regarded as a significant general-purpose biological oxidizing agent. Step-by-Step Solution: Classify NAD+ and FAD as canonical oxidants in dehydrogenase reactions.Recognize O2 as the terminal oxidant of aerobic ETC.Note Fe3+ is protein-bound (e.g., cytochromes), not a typical independent cellular oxidant.Select Fe3+ as the least appropriate choice. Verification / Alternative check: Standard biochemistry texts list NAD+/FAD and O2 as principal oxidants in cytosolic and mitochondrial metabolism; iron participates as cofactors rather than free oxidizing equivalents. Why Other Options Are Wrong: NAD+ is a primary oxidant accepting hydride ions in numerous pathways. FAD serves similarly in certain dehydrogenases. O2 is the terminal oxidant in aerobic organisms. Common Pitfalls: Confusing protein-bound electron carriers (e.g., cytochromes containing Fe) with freely diffusing oxidants like NAD+ or O2. Final Answer: Fe3+

Oxidative Phosphorylation Questions