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

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

Figure 22-34 Proton pump of bacteriorhodopsin. Page 825

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

Figure 22-36 Interpretive 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 22-36b Electron 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 22-37 Electron microscopy–based image of E. coli F1F0–ATPase. Page 828

Figure 22-38 X-Ray structure of F1–ATPase from bovine heart mitochondria. (a) A ribbon diagram. Page 828

Figure 22-38b X-Ray structure of F1–ATPase from bovine heart mitochondria. (b) Cross section through the electron density map of the protein. Page 828

Figure 22-38c X-Ray structure of F1–ATPase from bovine heart mitochondria. (c) The surface of the inner portion of the 33 assembly. Page 828

Figure 22-39 The , , and  subunits in the X-ray structure of bovine F1–ATPase. Page 829

Figure 22-40 NMR structures of the c subunit of E. coli F1F0–ATPase. Page 830

Figure 22-41a Low (3.9 Å) resolution electron density map of the yeast mitochondrial F1–c10 complex. (a) A view from within the inner mitochondrial membrane with the matrix above. Page 830

Figure 22-41b Low (3.9 Å) resolution electron density map of the yeast mitochondrial F1–c10 complex. (b) View from the intermembrane space of the boxed section of the c10 ring in the inset of Part a. Page 830

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

Figure 22-43 Model of the E. coli F1F0–ATPase. Page 832

Figure 22-44a Rotation of the c-ring in E. coli F1F0–ATPase. (a) The experimental system used to observe the rotation. Page 832

Figure 22-44b Rotation of the c-ring in E. coli F1F0–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

Figure 22-45 Stepwise rotation of the  subunit of F1 relative to an immobilized 33 unit at low ATP concentration as observed by fluorescence microscopy. Page 833

Figure 22-46 Uncoupling of oxidative phosphorylation. Page 834

Figure 22-47 Mechanism of hormonally induced uncoupling of oxidative phosphorylation in brown fat mitochondria. Page 835

Figure 22-48 Schematic diagram depicting the coordinated control of glycolysis and the citric acid cycle by ATP, ADP, AMP, Pi, Ca2+, and the [NADH]/[NAD+] ratio (the vertical arrows indicate increases in this ratio). Page 837

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

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