Unit 4 • Energetics & Respiration
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Do firstThermo & ∆G
1st Law: energy conserved. 2nd Law: every transfer increases entropy (heat loss). ∆G < 0 → spontaneous/exergonic; ∆G > 0 → endergonic.
Energy coupling: ATP hydrolysis drives endergonic steps via phosphorylation; phosphorylated intermediates become more reactive.
Enzymes & Inhibition
Enzymes lower Ea; do not change ∆G or equilibrium.
Regulation: allosteric effectors, covalent mods (phosphorylation), feedback inhibition.
Temperature/pH and substrate concentration shift rate; carriers saturate similar to enzymes.
Competitive
- • Binds active site; resembles substrate
- • High substrate can outcompete
- • Vmax unchanged; Km increases (need more substrate)
Noncompetitive/allosteric
- • Binds other site → shape change
- • Adding substrate cannot restore full rate
- • Lowers effective enzyme concentration; Vmax drops
Respiration Flow
Track electronsNAD⁺ → NADH
Reduced with H⁻; carries high-energy electrons to ETC (3 ATP per pair theoretical).
FAD → FADH₂
Enters ETC at complex II; yields ~2 ATP per pair theoretical.
Inhibitor logic: block complex IV (cyanide) → no O₂ reduction → no gradient → ATP synthase stops. Uncouplers leak H⁺ → heat instead of ATP.