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

1
Figure 22-1 The sites of electron transfer that
form NADH and FADH2 in glycolysis and the citric
acid cycle.
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Figure 22-9 The mitochondrial electron-transport
chain.
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Figure 22-11 Effect of inhibitors on electron
transport.
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Figure 22-12 Electron micrographs of mouse liver
mitochondria. (a) In the actively respiring
state. (b) In the resting state.
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Figure 22-13 Determination of the stoichiometry
of coupled oxidation and phosphorylation (the P/O
ratio) with different electron donors.
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Figure 22-14The mitochondrial electron-transport
chain.
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Figure 22-15 Structures of the common ironsulfur
clusters. (a) FeS cluster. (b) 2Fe2S
cluster. (c)4Fe4S cluster.
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Figure 22-17 Oxidation states of the coenzymes of
complex I. (a) FMN. (b) CoQ.
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Figure 22-20 Active site interactions in the
proposed mechanism of the QFR-catalyzed reduction
of fumarate to succinate.
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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.
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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.
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Figure 22-22a Porphyrin rings in cytochromes.
(a) Chemical structures.
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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 complexs redox centers.
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Figure 22-28 Proposed reaction sequence for the
reduction of O2 by the cytochrome a3CuB
binuclear complex of cytochrome c oxidase.
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Figure 22-29 Coupling of electron transport
(green arrow) and ATP synthesis.
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Figure 22-30 The redox loop mechanism for
electron transportlinked H translocation.
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Figure 22-31The Q cycle.
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Figure 22-33 Proton pump mechanism of electron
transportlinked proton translocation.
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Figure 22-34 Proton pump of bacteriorhodopsin.
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Figure 22-35 The proton-translocating channels in
bovine COX.
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Figure 22-36 Interpretive drawings of the
mitochondrial membrane at various stages of
dissection.
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Figure 22-36 Electron micrographs of the
mitochondrial membrane at various stages of
dissection. (a) Cristae from intact mitochondria
showing their F1 lollipops projecting into the
matrix. (b) Submitochondrial particles, showing
their outwardly projecting F1 lollipops.
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Figure 22-38a 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 22-41a 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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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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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 22-46 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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