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

Figure Effect of inhibitors on electron transport. Page 805

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

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

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

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

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

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

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

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

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

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

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

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

Figure 22-3 The Q cycle. Page 823

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

Figure 22-34Proton pump of bacteriorhodopsin. Page 825

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

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

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.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Figure 22-46Uncoupling of oxidative phosphorylation. Page 834

Figure 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

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