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Figure 12.01 Oxidative phosphorylation in context.

Figure 12.01 Oxidative phosphorylation in context. Figure 12.02 Model of mitochondrial structure. Figure 12.03a Images of mitochondria. Figure 12.03b Images of mitochondria. Figure 12.04 Micrograph of a mitochondrial network. Figure 12.05 The malate-aspartate shuttle system.

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Figure 12.01 Oxidative phosphorylation in context.

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  1. Figure 12.01 Oxidative phosphorylation in context.

  2. Figure 12.02 Model of mitochondrial structure.

  3. Figure 12.03a Images of mitochondria.

  4. Figure 12.03b Images of mitochondria.

  5. Figure 12.04 Micrograph of a mitochondrial network.

  6. Figure 12.05 The malate-aspartate shuttle system.

  7. Figure 12.06 Mitochondrial transport systems.

  8. Figure 12.07 Structure of Complex I determined by cryoelectron microscopy.

  9. Figure 12.08 Flavin mononucleotides (FMN).

  10. Figure 12.09 Iron-sulfur clusters.

  11. Figure 12.10 Complex I functions.

  12. Figure 12.11 Reactions that contribute to the ubiquinol pool.

  13. Figure 12.12 The heme group of a b cytochrome.

  14. Figure 12.13 X-Ray structure of mammalian Complex III.

  15. Figure 12.14 The Q cycle.

  16. Figure 12.15 Complex III function.

  17. Figure 12.16 Cytochrome c from tuna.

  18. Figure 12.17 X-Ray structure of cytochrome c oxidase.

  19. Figure 12.19 Complex IV function.

  20. Figure 12.20 Generation of a proton gradient.

  21. Figure 12.21 ATP synthase function.

  22. Figure 12.22a Structure of ATP synthase.

  23. Figure 12.22b Structure of ATP synthase.

  24. Figure 12.22c Structure of ATP synthase.

  25. Figure 12.23 Model for proton transport by Fo.

  26. Figure 12.24 Structure of the F1 component of ATP synthase.

  27. Figure 12.25 The binding change mechanism.

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