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BIOCHEM CH 11
Final exam
| Question | Answer |
|---|---|
| oxidative phosphorylation | coupled energy and electron transfer |
| electron transfer | FADH2 and NADH donate electrons to oxygen to produce water and provide energy for proton pump |
| energy transfer | FADH2 and NADH facilitate the phosphorylation of ADP to ATP |
| Net reaction | 10 NADH and FADH2 are oxidized to provide energy for proton pumping, 6O2 is reduced to produce 12 H20, 34 ATP produced |
| electron transport chain | flow of electrons from NADH and FADH2 to oxygen in aerobic respiration, oxygen generates energy for proton gradient |
| ATP production | proton gradient is used to power ATP synthase |
| ETC complexes | clustered in a respirasome, reversibly reduced and oxidized in inner mitochondrial membrane |
| which complexes pass through the membrane and pump protons? | CI, CIII, and CIV |
| which complex does not pass through the membrane and does not pump protons? | CII |
| Complex I: NADH-Q oxidoreductase complex | transfers electrons from NADH to ubiquinone, oxidation of the complex provides energy to pump 4 H+ for every 2 e- |
| Complex II: succinate- Q reductase complex | transfers electrons from FADH2 to ubiquinone, electrons come from conversion to succinate to fumarate in the CAC cycle |
| Complex III: Q-cytochrome c oxidoreductase complex | transfers electrons for CoQ to cytochrome c, oxidation of the complex provides energy to pump 4 H+ for every 2 e- |
| Complex IV: cytochrome c oxidase complex | transfers electrons from cytochrome c to O2, oxidation of the complex provides energy to pump 2 H+ for every 2 e- |
| ubiquinone | shuttles electrons and energy from CI and CII to CIII |
| O2 | final electron acceptor in complex IV |
| Standard reduction potential (E0') | affinity for electrons, more potential to be reduced |
| delta E0' | E0' products - E0' reactants |
| + change in E0' | more reduction potential in products, reaction moves to the right |
| - change in E0' | more reduction potential in reactants, reaction moves to the left |
| E0' and G0' | inversely related |
| spontaneous | + E0' and - G0' |
| non-spontaneous | - E0' and + G0' |
| equilibrium | E0' and G0' = 0 |
| electrons are more likely to be transferred to a biomolecule with a larger E0' because | it has greater electron affinity |
| NADH: lowest to greatest E0' | CI<CIII<CIV |
| FADH2: lowest to greatest E0' | CII<CIII<CIV |
| barbituates | block CI so electrons are not transferred and proton pumping from CI does not occur, CII-CIV can still occur |
| cyanide | blocks IV, backs up whole system |
| proton motive force | pH gradient and electric potential |
| pH gradient | proton concentration gradient between the matrix (low) and inner membrane space (high) |
| electric potential | separation of charge across the membrane |
| ATP synthase | converts energy from proton motive force into ATP |
| ATP synthase: F1 component | three sites of catalysis, in the matrix, hydrophilic, held to membrane by F0 |
| F1 structure | stalk made of gamma and epsilon subunits, 3 alpha and beta subunits alternate, delta subunit binds to F0 |
| ATP synthase: F0 component | integral inner mitochondrial membrane protein, hydrophobic around outside, contains H+ channel |
| F0 structure | a subunit, 2 b subunits connect A to delta of F1, c ring made of 8-15 subunits |
| F1 and F0 connection | gamma stalk and exterior column through a, 2b, and delta |
| what portions of ATP synthase remain in the membrane after salt wash? | salt water disrupts electrostatic interactions so it would disrupt the F1 component |
| ATP synthase: static portion | alpha and beta subunits |
| ATP synthase: rotating portion | c ring and gamma shaft |
| ATP synthase mechanism: 1) H+ rotates c ring of F0 part 1 | -when H+ concentration is high, H+ enters tunnel on inter-membrane space side of subunit a -H+ binds to glu or asp of c ring, making it hydrophobic - c subunit moves to lipid tails - H+ bound to c subunits pushed through to mitochondrial matrix |
| ATP synthase mechanism: 1) H+ rotates c ring of F0 part 2 | -when H+ are low in matrix, H+ dissociate and enter matrix, c ring is hydrophilic -ring movement turns c subunit to subunit a facing the inner-membrane space |
| ATP synthase mechanism: 2) c ring rotation makes gamma shaft rotate | curved gamma shaft bumps alpha and beta subunits causing catalytic change |
| ATP synthase mechanism: 3) binding change mechanism | beta subunit conformation change from gamma shaft rotation, changes affinity for ATP, ADP and Pi |
| open conformation (1) | ATP is released, ADP and Pi bind beta subunit |
| loose conformation (2) | nucleotides trapped in beta subunit |
| tight conformation (3) | ATP synthesized from ADP and Pi |
| ATP transport | ATP-ADP translocase and Phosphate translocase |
| ATP-ADP translocase | antiporter, 1 ATP out for every ADP in |
| Phosphate translocase | symporter, phosphate enters matrix with protons traveling down their chemical gradient |
| how many ATP come from ox phos? | 26 ATP |
Created by:
r.logan6029
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