2. Exam W 2/24 6-8 pm Review W afternoon? Feb 23, 2010 18:30-20:30 - Sigma Xi-CST lecture, Fraser 4 - Understanding Cancer Progression: Bringing Biology and Mathematics to the Challenge Alyssa Weaver

3. Figure 22-11 Effect of inhibitors on electron transport. Page 805

4. Figure 22-12 Electron micrographs of mouse liver mitochondria. (a) In the actively respiring state. (b) In the resting state. Page 806

5. Figure 22-13Determination of the stoichiometry of coupled oxidation and phosphorylation (the P/O ratio) with different electron donors. Page 807

6. Figure 22-14The mitochondrial electron-transport chain. Page 808

7. Figure 22-15 Structures of the common iron–sulfur clusters. (a) [Fe–S] cluster. (b) [2Fe–2S] cluster. (c)[4Fe–4S] cluster. Page 808

8. Figure 22-17 Oxidation states of the coenzymes of complex I. (a) FMN. (b) CoQ. Page 810

9. Figure 22-21aVisible absorption spectra of cytochromes. (a) Absorption spectrum of reduced cytochrome c showing its characteristic a, b, and g (Soret) absorption bands. Page 813

10. Figure 22-21Visible absorption spectra of cytochromes. (b) The three separate a bands in the visible absorption spectrum of beef heart mitochondrial membranes (below) indicate the presence of cytochromes a, b, and c. Page 813

11. Figure 22-22aPorphyrin rings in cytochromes. (a) Chemical structures. Page 813

12. Figure 22-25cX-Ray structure of fully oxidized bovine heart cytochrome c oxidase. (c) A protomer viewed similarly to Part a showing the positions of the complex’s redox centers. Page 816

13. Figure 22-28Proposed reaction sequence for the reduction of O 2 by the cytochrome a 3 –Cu B binuclear complex of cytochrome c oxidase. Page 819

14. Figure 22-29Coupling of electron transport (green arrow) and ATP synthesis. Page 821

15. Figure 22-30The redox loop mechanism for electron transport–linked H + translocation. Page 822

16. Figure 22-3 The Q cycle. Page 823

17. Figure 22-33Proton pump mechanism of electron transport–linked proton translocation. Page 825

18. Figure 22-34Proton pump of bacteriorhodopsin. Page 825

19. Figure 22-35 The proton- translocating channels in bovine COX. Page 826

20. Figure 22-36Interpretive drawings of the mitochondrial membrane at various stages of dissection. Page 827

21. Figure 22-36a Electron micrographs of the mitochondrial membrane at various stages of dissection. (a) Cristae from intact mitochondria showing their F1 “lollipops” projecting into the matrix.

22. Figure 22-36bElectron micrographs of the mitochondrial membrane at various stages of dissection. (b) Submitochondrial particles, showing their outwardly projecting F1 lollipops. Page 827

23. Figure 22-36c Electron micrographs of the mitochondrial membrane at various stages of dissection. (c) Submitochondrial particles after treatment with urea.

24. Figure 22-37Electron microscopy– based image of E. coli F 1 F 0 –ATPase. Page 828

25. Figure 22-38 X-Ray structure of F 1 –ATPase from bovine heart mitochondria. (a) A ribbon diagram. Page 828

26. Figure 22- 38bX-Ray structure of F 1 –ATPase from bovine heart mitochondria. (b) Cross section through the electron density map of the protein. Page 828

27. Figure 22-38cX-Ray structure of F 1 – ATPase from bovine heart mitochondria. (c) The surface of the inner portion of the  3  3 assembly. Page 828

28. Figure 22-39 The , , and  subunits in the X-ray structure of bovine F 1 – ATPase. Page 829

29. Figure 22-40 NMR structures of the c subunit of E. coli F 1 F 0 – ATPase. Page 830

30. Figure 22-41a Low (3.9 Å) resolution electron density map of the yeast mitochondrial F 1 –c 10 complex. (a) A view from within the inner mitochondrial membrane with the matrix above. Page 830

31. Figure 22-41bLow (3.9 Å) resolution electron density map of the yeast mitochondrial F 1 –c 10 complex. (b) View from the intermembrane space of the boxed section of the c 10 ring in the inset of Part a. Page 830

32. Figure 22-42Energy-dependent binding change mechanism for ATP synthesis by proton-translocating ATP synthase. Page 831

33. Figure 22-43Model of the E. coli F 1 F 0 –ATPase. Page 832

34. Figure 22-44aRotation of the c-ring in E. coli F 1 F 0 –ATPase. (a) The experimental system used to observe the rotation. Page 832

35. Figure 22-44bRotation of the c-ring in E. coli F 1 F 0 –ATPase. (b) The rotation of a 3.6-  m-long actin filament in the presence of 5 mM MgATP as seen in successive video images taken through a fluorescence microscope. Page 832

36. Movies http://atom.chem.wwu.edu/sacahill/472/atp %20synthase.movhttp://atom.chem.wwu.edu/sacahill/472/atp %20synthase.mov http://atom.chem.wwu.edu/sacahill/472/atp %20synthase2.movhttp://atom.chem.wwu.edu/sacahill/472/atp %20synthase2.mov http://atom.chem.wwu.edu/sacahill/472/rot arymech.movhttp://atom.chem.wwu.edu/sacahill/472/rot arymech.mov

37. Figure 22-46Uncoupling of oxidative phosphorylation. Page 834

38. Figure 22-48 Schematic diagram depicting the coordinated control of glycolysis and the citric acid cycle by ATP, ADP, AMP, P i, Ca 2+, and the [NADH]/[NAD + ] ratio (the vertical arrows indicate increases in this ratio). Page 837

39. “Alfonse, Biochemistry makes my head hurt!!” \