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BIOLOGICAL OXIDATION
[object Object],[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]
ATP as an ENERGY CARRIER ,[object Object],[object Object],[object Object]
Energy carried by ATP ,[object Object],[object Object],[object Object],[object Object],[object Object]
ELECTRON TRANSPORT CHAIN ,[object Object],[object Object],[object Object],[object Object]
Site of ETC ,[object Object],[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]
Organization of the chain ,[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]
 
Reactions of the electron transport chain ,[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object]
Release of free energy during ETC:- ,[object Object],[object Object],[object Object],[object Object]
 
[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],Cytochromes
[object Object],[object Object],[object Object],Heme  is a prosthetic group of  cytochromes .  Heme contains an iron atom in a porphyrin ring system.
[object Object],[object Object],[object Object],[object Object],[object Object],Electron carriers
ETC ---- REVIEW ,[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object]
 
Electron Carriers NAD +  or  FAD There are 2 sites of entry for electrons into the electron transport chain:  Both are coenzymes for dehydrogenase enzymes The transfer of electrons is not directly to oxygen but through coenzymes
Inhibitors of ETC ,[object Object],[object Object],[object Object]
[object Object],[object Object]
H +  Transport ,[object Object],[object Object],[object Object]
[object Object],[object Object]
[object Object]
[object Object],[object Object],[object Object],[object Object]
Release of free energy during ETC  ,[object Object],[object Object],[object Object]
Reduction Potentials Number of electrons transferred in the redox reaction Faraday’s constant (96485 J/volt/mole) Crucial equation:    G o ' = -n F    E o '   The relative tendency to accept e - s and become reduced.   = E o '(acceptor) - E o '(donor) E 0 ’=standard reduction potential. If     E o '  is positive, an electron transfer reaction is  spontaneous (  G o ' <0)
OXIDATIVE PHOSPHORYLATION
[object Object],[object Object],[object Object]
Chemiosmotic hypothesis of ATP synthesis  ,[object Object],[object Object]
ATP synthase ,[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object]
Inhibition of Oxidative Phosphorylation ,[object Object],[object Object],[object Object],[object Object]
Uncouplers of oxidative phosphorylation ,[object Object],[object Object],[object Object]
Transport of ADP and ATP  ,[object Object],[object Object]
Transport of reducing equivalents ,[object Object],[object Object]
CYTOPLASM OUTER MEMBRANE MATRIX INNER MEMBRANE Figure 3.   The malate-aspartate shuttle.  OAA Malate (1) e - NAD + e - Glu 0 (6) Glu 0 Asp -1 (4) KG KG Malate (2) e - e - OAA NADH NAD + (3) e - Complex I e - NAD + Glucose Pyruvate GLYCOLYSIS NADH Asp -1 (5)
CYTOPLASM INNER MEMBRANE MATRIX FAD Glycerol-3-phosphate  dehydrogenase (2) DHAP OUTER MEMBRANE Figure 4.  Glycerol phosphate shuttle.  Cytoplasmic glycerol 3-phosphate dehydrogenase (1) oxidizes NADH. Glycerol 3-phosphate dehydrogenase in the inner membrane (2) reduces FAD to FADH 2 . G3P Dihydroxyacetone phosphate (DHAP) NAD + 3-phosphate Glycerol e  (1) FADH 2 e  CoQ e  O 2 e  NADH Glucose Pyruvate GLYCOLYSIS NAD +

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Biological oxidation

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  • 26. Electron Carriers NAD + or FAD There are 2 sites of entry for electrons into the electron transport chain: Both are coenzymes for dehydrogenase enzymes The transfer of electrons is not directly to oxygen but through coenzymes
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  • 34. Reduction Potentials Number of electrons transferred in the redox reaction Faraday’s constant (96485 J/volt/mole) Crucial equation:   G o ' = -n F  E o ' The relative tendency to accept e - s and become reduced.  = E o '(acceptor) - E o '(donor) E 0 ’=standard reduction potential. If  E o ' is positive, an electron transfer reaction is spontaneous (  G o ' <0)
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  • 44. CYTOPLASM OUTER MEMBRANE MATRIX INNER MEMBRANE Figure 3. The malate-aspartate shuttle. OAA Malate (1) e - NAD + e - Glu 0 (6) Glu 0 Asp -1 (4) KG KG Malate (2) e - e - OAA NADH NAD + (3) e - Complex I e - NAD + Glucose Pyruvate GLYCOLYSIS NADH Asp -1 (5)
  • 45. CYTOPLASM INNER MEMBRANE MATRIX FAD Glycerol-3-phosphate dehydrogenase (2) DHAP OUTER MEMBRANE Figure 4. Glycerol phosphate shuttle. Cytoplasmic glycerol 3-phosphate dehydrogenase (1) oxidizes NADH. Glycerol 3-phosphate dehydrogenase in the inner membrane (2) reduces FAD to FADH 2 . G3P Dihydroxyacetone phosphate (DHAP) NAD + 3-phosphate Glycerol e  (1) FADH 2 e  CoQ e  O 2 e  NADH Glucose Pyruvate GLYCOLYSIS NAD +