Oxidative Phosphorylation

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Presentation transcript:

Oxidative Phosphorylation Chapter 11 Oxidative Phosphorylation

11.1 The Chemiosmotic Theory, Part 1 Copyright © 2017 W. W. Norton & Company

11.1 The Chemiosmotic Theory, Part 2 Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Proton Flow Copyright © 2017 W. W. Norton & Company

Electron Transport System (Chain) Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Proton Circuit Copyright © 2017 W. W. Norton & Company

Energy Transformations in Oxidative Phosphorylation View the Energy Transformations in Oxidative Phosphorylation animation Copyright © 2017 W. W. Norton & Company

Proton Uncoupling Effects Copyright © 2017 W. W. Norton & Company

Mitochondrial Structure Copyright © 2017 W. W. Norton & Company

Protein Components of the Electron Transport System Complex Protein Complex I NADH – ubiquinone oxidoreductase Complex II Succinate dehydrogenase Complex III Ubiquinone-cytochrome c oxidoreductase Complex IV Cytochrome oxidase Complex V ATP synthase complex Copyright © 2017 W. W. Norton & Company

Electron Transport System Copyright © 2017 W. W. Norton & Company

11.2 Mitochondrial Electron Transport System – 1 Copyright © 2017 W. W. Norton & Company

11.2 Mitochondrial Electron Transport System – 2 Copyright © 2017 W. W. Norton & Company

Electron Transport System Inhibitors Copyright © 2017 W. W. Norton & Company

Redox Potentials and the Electron Transport System Electron carriers Standard Reduction Potentials in Volts Positive NAD plus positive 1 Hydrogen ion plus 2 electrons yields NADH Negative 0.32 Complex 1 left parenthesis NADH-ubiquinone oxidoreductase right parenthesis: Iron-Sulfur left parenthesis N-1b right parenthesis Negative 0.25 Complex 1 left parenthesis NADH-ubiquinone oxidoreductase right parenthesis: Iron-Sulfur left parenthesis N-3,4 right parenthesis Negative 0.24 Complex 1 left parenthesis NADH-ubiquinone oxidoreductase right parenthesis: Iron-Sulfur left parenthesis N-5.6 right parenthesis Negative 0.27 Complex 2 left parenthesis succinate dehydrogenase right parenthesis: FAD plus 2 positive 1 Hydrogen ion plus 2 electrons yields FADH 2 left parenthesis enzyme bound right parenthesis Negative 0.04 Complex 2 left parenthesis succinate dehydrogenase right parenthesis: Iron-Sulfur left parenthesis S-1 right parenthesis Negative 0.03 Complex 2 left parenthesis succinate dehydrogenase right parenthesis: Cytochrome b 560 Negative 0.08 Complex 2 left parenthesis succinate dehydrogenase right parenthesis: Coenzyme Q plus 2 positive 1 Hydrogen ion plus 2 electrons Positive 0.04 Complex 3 left parenthesis ubiquinone-cytochrome c oxidoreductase right parenthesis: Cytochrome b H Positive 0.03 Complex 3 left parenthesis ubiquinone-cytochrome c oxidoreductase right parenthesis: Cytochrome b L Complex 3 left parenthesis ubiquinone-cytochrome c oxidoreductase right parenthesis: Iron-Sulfur Positive 0.28 Complex 3 left parenthesis ubiquinone-cytochrome c oxidoreductase right parenthesis: Cytochrome c 1 Positive 0.21 Complex 3 left parenthesis ubiquinone-cytochrome c oxidoreductase right parenthesis: Cytochrome c left parenthesis Upper C-y-t c right parenthesis Positive 0.23 Complex 4 left parenthesis cytochrome c oxidase right parenthesis: Cytochrome a Complex 4 left parenthesis cytochrome c oxidase right parenthesis: Copper A Positive 0.24 Complex 4 left parenthesis cytochrome c oxidase right parenthesis: Cytochrome a 3 Positive 0.38 Complex 4 left parenthesis cytochrome c oxidase right parenthesis: One-half Upper O 2 plus 2 positive 1 Hydrogen ions yields Upper H 2 Upper O Positive 0.82 Copyright © 2017 W. W. Norton & Company

Redox Loops and Proton Pumps Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Complex I Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Complex I Structure Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company FMN Reactions Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Coenzyme Q Function Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Coenzyme Q Reduction Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Complex II Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Complex III Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Q Cycle Copyright © 2017 W. W. Norton & Company

Cytochrome Structures Figure 11.20 Cytochrome proteins are classified as type a, type b, and type c according to the type of heme they contain. The heme group of cytochrome c is covalently linked to the protein through thiol groups from cysteine residues, whereas the type a heme has a long hydrophobic tail. Copyright © 2017 W. W. Norton & Company

Copyright © 2017 W. W. Norton & Company Complex IV Copyright © 2017 W. W. Norton & Company

Bioenergetics of the Proton-Motive Force Copyright © 2017 W. W. Norton & Company

11.3 Structure and Function of the ATP Synthase Complex Copyright © 2017 W. W. Norton & Company

Detailed Structure of ATP Synthase Complex Copyright © 2017 W. W. Norton & Company

ATP Synthase View the ATP Synthase animation Copyright © 2017 W. W. Norton & Company

Conformational Changes in ATP Synthase Copyright © 2017 W. W. Norton & Company

Binding Changes during ATP Synthesis in ATP Synthase Copyright © 2017 W. W. Norton & Company

Experiment Showing ATP Synthase Is a Molecular Motor Copyright © 2017 W. W. Norton & Company