Topic 3: Cellular Energetics

College Board AP Biology · 0 min read

Every living cell runs on a constant flow of energy. Unit 3 traces that flow from the molecules that speed up chemical change (enzymes) to the universal energy currency (ATP) and finally to the two great pathways that move energy through the biosphere: photosynthesis, which stores light energy in the bonds of organic molecules, and cellular respiration, which releases that stored energy to power life. A recurring theme is that these processes are governed by the laws of thermodynamics and are exquisitely sensitive to environmental conditions such as temperature and pH.

Enzyme Structure and Catalysis

Enzymes are biological catalysts, usually proteins, that speed up reactions without being consumed. Each enzyme has an active site whose three-dimensional shape is complementary to a specific substrate. Specificity comes from this shape and chemistry match. The favored model is induced fit: substrate binding causes the active site to change shape slightly, gripping the substrate and straining its bonds. Because enzyme structure determines function, anything that disrupts the active site's shape reduces or eliminates activity.

Activation Energy and Reaction Rate

Even spontaneous (energetically favorable) reactions need an initial input of energy, the activation energy, to break existing bonds and reach the transition state. Enzymes work by lowering activation energy, allowing far more substrate molecules to react at biological temperatures. Enzymes do not change whether a reaction is exergonic or endergonic and do not alter the overall free-energy change (ΔG); they only change the rate by providing a lower-energy path.

Environmental Effects on Enzymes

Enzyme activity depends on conditions. Each enzyme has an optimal temperature and optimal pH; activity rises toward the optimum and falls beyond it. Excessive heat or extreme pH disrupts the bonds maintaining protein shape, causing denaturation, a loss of the functional 3-D structure. Increasing substrate concentration raises rate until enzymes are saturated, after which rate plateaus. Adding more enzyme (with ample substrate) also raises rate.

Enzyme Inhibition and Regulation

Competitive inhibitors resemble the substrate and bind the active site, blocking substrate entry; their effect can be overcome by adding more substrate. Noncompetitive (allosteric) inhibitors bind a site other than the active site, changing the enzyme's shape so the active site no longer functions well; adding substrate does not reverse this. Cells also use feedback inhibition, in which a pathway's end product binds an early enzyme to shut the pathway down once enough product accumulates.

ATP and Coupled Reactions

ATP (adenosine triphosphate) is the cell's energy currency. Hydrolysis of its terminal phosphate bond releases energy and yields ADP + inorganic phosphate. This exergonic release is used to drive endergonic reactions through energy coupling, often by transferring the phosphate to another molecule (phosphorylation). ATP is continually regenerated from ADP using energy from cellular respiration, making it a renewable, short-term energy carrier rather than long-term storage.

Photosynthesis: Overview and Light Reactions

Photosynthesis converts light energy into chemical energy in chloroplasts. In the light-dependent reactions on the thylakoid membranes, chlorophyll in photosystems II and I absorbs light, exciting electrons. Water is split (photolysis), releasing O₂ and supplying replacement electrons and protons. Electrons travel down an electron transport chain, pumping H⁺ into the thylakoid lumen; this proton gradient powers ATP synthase to make ATP (photophosphorylation), and NADP⁺ is reduced to NADPH.

Photosynthesis: The Calvin Cycle

The Calvin cycle (light-independent reactions) occurs in the stroma and uses the ATP and NADPH from the light reactions to build sugar. The enzyme rubisco fixes CO₂ onto RuBP (carbon fixation). The resulting molecules are reduced using NADPH and energized by ATP to form G3P, a three-carbon sugar; some G3P leaves to make glucose while the rest regenerates RuBP. Though called light-independent, the cycle depends on products supplied by the light reactions.

Cellular Respiration: Glycolysis and the Krebs Cycle

Glycolysis, in the cytoplasm, splits glucose into two pyruvate molecules, producing a net 2 ATP (by substrate-level phosphorylation) and 2 NADH; it requires no oxygen. With oxygen present, pyruvate is oxidized to acetyl-CoA (releasing CO₂ and making NADH). The Krebs (citric acid) cycle in the mitochondrial matrix fully oxidizes acetyl-CoA, releasing CO₂ and harvesting energy as NADH, FADH₂, and a small amount of ATP.

Electron Transport Chain and Chemiosmosis

NADH and FADH₂ deliver high-energy electrons to the electron transport chain on the inner mitochondrial membrane. As electrons pass down the chain, energy is used to pump H⁺ into the intermembrane space, building an electrochemical gradient. In chemiosmosis, protons flow back through ATP synthase, driving oxidative phosphorylation to produce most of the cell's ATP. Oxygen is the final electron acceptor, combining with electrons and H⁺ to form water; without it, the chain backs up and stops.

Fermentation and Anaerobic Pathways

When oxygen is absent, the electron transport chain cannot run, so NADH cannot be reoxidized there. Fermentation regenerates NAD⁺ so glycolysis can continue producing a small amount of ATP. In lactic acid fermentation (some animal and muscle cells), pyruvate is reduced to lactate. In alcohol fermentation (yeast, some microbes), pyruvate is converted to ethanol and CO₂. Fermentation yields far less ATP than aerobic respiration but allows survival without oxygen.

Key terms

Enzyme
A biological catalyst, usually a protein, that lowers activation energy and speeds reactions without being consumed.
Active site
The region of an enzyme where substrate binds and catalysis occurs, with a shape complementary to the substrate.
Substrate
The reactant molecule an enzyme acts upon.
Induced fit
Model in which substrate binding slightly reshapes the active site to grip the substrate more tightly.
Activation energy
The energy input required to start a reaction by reaching the transition state; enzymes lower it.
Denaturation
Loss of a protein's functional 3-D shape, often caused by extreme temperature or pH.
Competitive inhibitor
A molecule that binds the active site and blocks the substrate; reversible by adding more substrate.
Noncompetitive inhibitor
A molecule that binds away from the active site, altering enzyme shape and reducing function.
Feedback inhibition
Regulation in which a pathway's end product inhibits an earlier enzyme to control output.
ATP
Adenosine triphosphate, the cell's energy currency; its hydrolysis to ADP releases usable energy.
Energy coupling
Using an exergonic reaction (such as ATP hydrolysis) to drive an endergonic reaction.
Light-dependent reactions
Thylakoid reactions that use light to make ATP and NADPH and release O₂ from water.
NADPH
An electron carrier produced in the light reactions that supplies reducing power to the Calvin cycle.
Calvin cycle
Stroma reactions that use ATP and NADPH to fix CO₂ and build the sugar G3P.
Rubisco
The enzyme that fixes CO₂ onto RuBP, beginning carbon fixation in the Calvin cycle.
Glycolysis
Cytoplasmic splitting of glucose into two pyruvate, yielding net 2 ATP and 2 NADH without oxygen.
Krebs cycle
Matrix pathway that oxidizes acetyl-CoA, releasing CO₂ and producing NADH, FADH₂, and ATP.
Electron transport chain
Inner-membrane carriers that pass electrons and pump H⁺ to build a proton gradient.
Chemiosmosis
Flow of H⁺ through ATP synthase down its gradient, driving ATP synthesis.
Oxidative phosphorylation
ATP production powered by chemiosmosis using energy from electron transport.
Fermentation
Anaerobic regeneration of NAD⁺ (forming lactate or ethanol) that lets glycolysis continue.

Exam technique

Quick check
A researcher adds a molecule to an enzyme reaction and finds that the inhibition cannot be overcome by increasing substrate concentration. What is the most likely explanation?
  1. The molecule is a competitive inhibitor binding the active site
  2. The molecule is a noncompetitive inhibitor binding outside the active site
  3. The molecule increased the activation energy of the reaction
  4. The molecule denatured the substrate rather than the enzyme
Show answer
Answer: 1. Because added substrate cannot reverse the effect, the inhibitor is not competing for the active site. A noncompetitive (allosteric) inhibitor binds a different site and changes the enzyme's shape, so flooding the system with substrate does not restore activity.

Test yourself

Practise exam-style questions on this topic.

Go to the quiz →
All study notes