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N"O,PQRSTEUV7W NADHE9B8XYZ[EU\];^]W__4W.`aQb9cdeE9
BWf_4TMPDbTgPhiQXEjB];_*bk*WTgPhiQX*lmKn7W.`aQEjB]opbjBq9op*ATPrs*tuEvwM;^]WXYZ[*tuxvwM;

Page 813!"#$%&'()*+,-./0123456789:; NADH<=+,-./0>*?@*AB*CDE
FG:HIEJKLM;

Figure 22-21a Visible absorption spectra of cytochromes.
(a) Absorption spectrum of reduced cytochrome c showing its
characteristic !, ", and # (Soret) absorption bands.

Page 813

Page 813&'()*+,-./!-0123456

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

Page 813

Figure 22-21b The three separate ! bands in the spectrum ofbeef heart mitochondrial membranes indicate the presence of
cytochromes a, b, and c.

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

Cytochrome C!"#Page 815

Page 814(a)(b)

Figure 22-23 X-ray structures of cytochrome bc1. (a) The dimericbovine complex. (b) The yeast enzyme in complex with cytochrome cFigure 22-24 Ribbon diagram of cytochrome c showing the Lys
residues involved in intermolecular complex formation.

Complex IV

Page 816

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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 complex’s redox centers.

789:;<=>?@ABC2DEFGHIJKLMNOPQRS:T

Page 819

Page 818

Figure 22-26 The redox
centers in the X-Ray
structure of bovine heart
cytochrome c oxidase.

Figure 22-27 Synthetic model of the cytochrome a3–CuBbinuclear complex.

Page 819

Page 822

Figure 22-30 The redox loop mechanism for electrontransport–linked H+ translocation.

Page 823

Figure 22-28 Proposed reaction sequence for the reduction of O2 by
the cytochrome a3–CuB binuclear complex of cytochrome c oxidase.

Figure 22-32a X-Ray structures of the Qo binding site of the chicken
cytochrome bc1 complex occupied by inhibitors. (a) This structure
shows its complex with stigmatellin.

Page 824

Page 824

Figure 22-31 The Q cycle.

Figure 22-32b X-Ray structures of the Qo binding site of the chickencytochrome bc1 complex occupied by inhibitors. (b) This structure
shows its complex with myxothiazol.

Page 825

Page 825

Figure 22-34 Proton
pump ofbacteriorhodopsin.

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

Page 827

Page 826

Figure 22-35 The protontranslocating channels inbovine COX.

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

Page 827

abc

Figure 22-36 Electron micrographs of cristae from (a) intact
mitochondria showing their F1 “lollipops” projecting into the matrix,(b) submitochondrial particles, showing their outwardly projecting F1
lollipops, and (c) submitochondrial particles after treatment with urea.

ATP synthase, a molecular machine(fig9-14)

FaATPase!"#$%&'()*+*,-.
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! " !

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#%
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Page 828

Page 828c10-12

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

Page 828

Page 828

Figure 22-37 Electron microscopy–based image of E. coli
F1F0–ATPase.

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

Figure 22-38c
X-Ray structure of F1–ATPase frombovine heart mitochondria. (c) The surface of the inner portion ofthe !3"3 assembly.

Page 829

Page 830

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

Page 830

Page 830

Figure 22-39 The #, $, and % subunits in the X-ray structureof bovine F1–ATPase.

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

Figure 22-41b
The electron density map of the yeast
mitochondrial F1–c10 complex. View of the boxed section inPart a from the intermembrane space.

Page 831

ATPase!"#b^5cdefghi

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

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!"#$%&'(/012,134#$%&'(/012,134!"/01234#5)&67#$%&'$()&*+,-.-89:89:BCD*E F GHIJ

Noji et al. (1997) NaturePage 832

8;:<:=>?@AFigure 22-44b
Rotation of the c-ring in E. coli
F1F0–ATPase. (b) The rotation of a 3.6-µm-long actin filamentin the presence of 5 mM MgATP.