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

1
Figure 22-29 Coupling of electron transport
(green arrow) and ATP synthesis.
Page 821
2
Figure 22-34 Proton pump of bacteriorhodopsin.
Page 825
3
Figure 22-35 The proton-translocating channels in
bovine COX.
Page 826
4
Figure 22-36 Interpretive drawings of the
mitochondrial membrane at various stages of
dissection.
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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.
6
Figure 22-36b Electron micrographs of the
mitochondrial membrane at various stages of
dissection. (b) Submitochondrial particles,
showing their outwardly projecting F1 lollipops.
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Figure 22-36c Electron micrographs of the
mitochondrial membrane at various stages of
dissection. (c) Submitochondrial particles after
treatment with urea.
8
Figure 22-37 Electron microscopybased image of
E. coli F1F0ATPase.
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Figure 22-38 X-Ray structure of F1ATPase from
bovine heart mitochondria. (a) A ribbon diagram.
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Figure 22-38b X-Ray structure of F1ATPase from
bovine heart mitochondria. (b) Cross section
through the electron density map of the protein.
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Figure 22-38c X-Ray structure of F1ATPase from
bovine heart mitochondria. (c) The surface of the
inner portion of the ?3?3 assembly.
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Figure 22-39 The ?, ?, and ? subunits in the
X-ray structure of bovine F1ATPase.
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Figure 22-40 NMR structures of the c subunit of
E. coli F1F0ATPase.
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Figure 22-41a Low (3.9 Å) resolution electron
density map of the yeast mitochondrial F1c10
complex. (a) A view from within the inner
mitochondrial membrane with the matrix above.
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15
Figure 22-41b Low (3.9 Å) resolution electron
density map of the yeast mitochondrial F1c10
complex. (b) View from the intermembrane space of
the boxed section of the c10 ring in the inset of
Part a.
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16
Figure 22-42 Energy-dependent binding change
mechanism for ATP synthesis by proton-translocatin
g ATP synthase.
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Figure 22-43 Model of the E. coli F1F0ATPase.
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Figure 22-44a Rotation of the c-ring in E. coli
F1F0ATPase. (a) The experimental system used to
observe the rotation.
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Figure 22-44b Rotation of the c-ring in E. coli
F1F0ATPase. (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.
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20
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.
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Figure 22-46 Uncoupling of oxidative
phosphorylation.
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Figure 22-47 Mechanism of hormonally induced
uncoupling of oxidative phosphorylation in brown
fat mitochondria.
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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).
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Alfonse, Biochemistry makes my head hurt!!
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