Oxidative Phosphorylation Frederick Stanley
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1 Oxidative Phosphorylation Frederick Stanley I) Introduction A) Glucose 1) A highly reduced molecule with much potential energy. 2) Substrate level oxidation yields only 4 ATPs. 3) 2 NADH are produced in the cytoplasm by glycolysis. 4) 8 NADH and 2 FADH 2 are produced in the mitochondria by the TCA cycle. B) ATP 1) ATP is the common currency of free energy in the cell. 2) A large amount is consumed: about 40 kg/day. II) Mitochondria A) Outer Membrane B) Inner Membrane C) Matrix D) DNA E) Enzymes (TCA cycle, beta-oxidation, oxidative phosphorylation) F) Mitochondrial diseases III) Transport between the mitochondrial matrix and the cytoplasm is tightly controlled. A) Specific carriers Name in Out ATP/ADP Translocase ADP 3- ATP 4- Pyruvate carrier Pyruvate - OH - Dicarboxylate carrier - PO 4 Malate/fumarate/succinate Tricarboxylate Carrier Citrate + H + malate Phosphate carrier - PO 4 OH - B) Transport of NADH from the cytoplasm into the mitochondrial matrix 1) Glycerol 3-phosphate shuttle 2) Malate aspartate shuttle IV) Bioenergetics A) Mitchel hypothesis 1) Electrons from NADH are donated, to oxygen via a series of redox reactions. 2) As electrons flow through the electron transport chain, protons are pumped from the mitochondrial matrix to the cytoplasm. 3) The transfer of protons generates an electrochemical gradient: a ph gradient of 1.4 ph units, and an electrical gradient of 150 mv. 4) The synthesis of ATP is driven by the flow of protons flow back into the mitochondrial matrix. 1
2 B) Electron carriers Oxidant Reductant E 0 NAD + NADH + H Ubiquinone QH Cytochrome c (+3) Cytochrome c (+2) /2 O H + H 2 O C) Energy 1) NADH oxidation: E 0 = V G 0 = kcal/mol of NADH 2) Proton gradient: ~ 5 kcal/mol of H + pumped X 10 H + pumped /NADH = ~50 kcal 3) ATP synthesis: ADP + Pi ATP 7.3 kcal/mol X 2.5 mol ATP / mol NADH = 18.3 kcal V) Important molecules A) NAD + / NADH + H + - resonance stabilization B) FAD / FADH 2 stable radical C) FMN / FMNH 2 stable radical D) Ubiquinone / QH 2 stable radical E) Iron-Sulfur proteins Redox potential altered by environment F) Cytochromes / Hemes Shift in absorption spectra dependent on red/ox state VI) Electron transport A) Overview 1) Regulation (a) Downhill flow of electrons (b) Build up of substrates 2) Inhibitors antimycin, CN, CO B) Complex I / NADH/Q reductase 1) Structure of the complex: (a) FMN (b) Iron-sulfur (c) Bound Quinone (d) Quinone pool (e) Mitochondrial derived proteins (f) Hydrophilic / Amphipathic / hydrophobic 2) Reaction: 2 electrons are transfered from NADH to Q via FMN and Fe-S 3) 4 H + are pumped from the matrix to the cytoplasm for each 2 e - from NADH 4) Mutations in mitochondrial DNA can lead to defects in electron transport. 2
3 C) Complex III / cytochrome reductase 1) Structure of the complex: (a) Rieske iron sulfur (b) Cytochrome (c) Cytochrome b (d) Quinone 2) Functions to convert 2 electron transfer to 1 electron transfer 3) 2 H + are pumped from the matrix to the cytoplasm for each 2e - of NADH D) Complex IV / Cytochrome oxidase 1) Structure of the complex: (a) CuA Cytochrome a (b) CuB Cytochrome a 3 2) Reaction: reduction of O 2 to H 2 O 3) 4 H + are pumped from the matrix to the cytoplasm for each 2e - of NADH E) Complex II / Succinate dehydrogenase; acyl CoA dehydrogenase 1) Structure- may be oldest; it is the most conserved from bacteria to mammal (a) Peripheral - FAD (b) Peripheral iron sulfur (c) Membrane anchored heme (d) Quinone 2) Reactions: (a) Succinate + FAD Fumarate + FADH 2 (b) AcylCoA + FAD Enoyl CoA + FADH 2 3) No H + is transported. (a) The oxidation of FADH 2 results in the pumping of 6 H + rather than 10 H + pumped per NADH + H + (b) About 1.5 ATP are formed /FADH 2 rather than about 2.5ATP/NADH+ H + VII) How are protons pumped? A) Conformational changes in the electron carrier proteins B) Direct transport of H + VIII) How is the electrochemical gradient converted to phosphoryl transfer potential? A) How ATP synthase works. 1) The enzyme is a biological motor coupling an H + channel and a molecular rotor. 2) Structure and function of the ATP synthase. 3) The rotor B) Regulation by ADP: in the cell, the ATP:ADP:AMP ratio is constant at about 20:1:0.1 3
4 Complex II - Succinate:quinone oxidoreductase Respiratory chain redox components in the inner membrane of bovine heart mtitochondria are schematically shown. Iron-sulfur clusters in the NADH-UQ (Complex I) and succinate-uq (Complex II) oxidoreductase segments are distinguished with suffixes Nx and Sx, respectively. Q N, Q S and (Qo and Qi) denote specific UQ binding sites in Complex I, Complex II, and ubiquinol-cytochrome c oxidoreductase (Complex III) segment, respectively. Specific inhibitor binding sites are illustrated with arrows. Redox midpoint potentials at ph 7 of Complex I components are also shown. 4
5 Complex I - NADH-Q reductase Complex II - Succinate:quinone oxidoreductase 5
6 Complex III Cytochrome bc1 1. QH 2 is oxidized: - one electron reduces heme of cytochrome b - one electron reduces Fe of the iron sulfur complex - two protons are released into the matrix 2. Internal electron transfers: - iron sulfur complex moves to cyt c c c c is reduced - heme is reduced 3. Electrons accepted - QH (semiquinone) is formed - one cytochrome c is reduced 2 H + Intermembrane space e - Cyt c e - QH 2 bl e - e - Q Mitochondrial matrix H + 4. Result at the end of the first half-cycle 5. Result of one full reaction cycle - 2 QH 2 oxidized to 2 Q - 1 Q reduced to 1 QH 2-2 cytochrome c reduced - 4 protons pumped out of matrix 2 H + Intermembrane space 4 H + Cyt c e Cyt c e - 2 QH 2 QH QH 2 H + Mitochondrial matrix 2 H + Mechanism by which complex III couples proton pumping to oxidation/reduction. Two molecules of QH 2 are oxidized to four protons and four electrons. The four protons are released from the cytosolic side of the membrane. Two of the four electrons reduce two cytochrome c. The other two electrons reduce one molecule of Q. 6
7 Complex IV - Cytochrome Oxidase The Mitochondrial ATPase 7
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