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
Exam W 2/ pm
Review W afternoon?

3. Isotopic Tests:
Generation of specifically labeled OAA

4. +CoASH CH3
CH3-
COO-
C=O
CoASH
When in the TCA cycle would this
label be lost as CO2?

5. Table 21-2 Standard Free Energy Changes (DG°¢) and Physiological Free Energy Changes (DG) of Citric Acid Cycle Reactions.
Page 790

6. Figure 21-25 Regulation of the citric acid cycle.
Page 791

7. Figure 21-26
Amphibolic
functions of the
citric acid cycle.
Page 793

8. Electron Transport and Oxidative Phosphorylation
Chapter 22:
Electron Transport and
Oxidative Phosphorylation

9. E + H+ + Fum  EH+ + Fum▪OH-E ▪ H+ ▪Mal-
OH carbanion
E + H+ + Fum  EH+ + Fum▪OH-E ▪ H+ ▪Mal-
 
18O exchange E + H+ + Mal

10. Figure 22-1 The sites of electron transfer that form NADH and FADH2 in glycolysis and the citric acid cycle.
Page 798

11. Figure 22-2a. Mitochondria
Figure 22-2a Mitochondria. (a) An electron micrograph of an animal mitochondrion.
Page 799

12. Figure 22-2b Mitochondria. (b) Cutaway diagram of a mitochondrion.
Page 799

13. Figure 22-3 Freeze-fracture and freeze-etch electron micrographs of the inner and outer mitochondrial membranes.
Page 799

14. Figure 22-7 The malate–aspartate shuttle.
Page 801

15. Figure 22-8 The glycerophosphate shuttle.
Page 802

16. Figure 22-9 The mitochondrial electron-transport chain.
Page 803

17. Table 22-1 Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria.
Page 806

18. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria.
Page 806

19. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria.
Page 806

20. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria.
Page 806

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

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

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

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

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

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

27. Figure Active site interactions in the proposed mechanism of the QFR-catalyzed reduction of fumarate to succinate.
Page 812

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

29. Figure 22-21Visible absorption spectra of cytochromes
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

30. Figure 22-22a Porphyrin rings in cytochromes. (a) Chemical structures.
Page 813
Figure 22-22a Porphyrin rings in cytochromes. (a) Chemical structures.

31. Figure 22-22b. Porphyrin rings in cytochromes
Figure 22-22b Porphyrin rings in cytochromes. (b) Axial liganding of the heme groups contained in cytochromes a, b, and c are shown.
Page 813

32. Page 816
Figure 22-25c X-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.

33. Figure Proposed reaction sequence for the reduction of O2 by the cytochrome a3–CuB binuclear complex of cytochrome c oxidase.
Page 819

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

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