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１１サブユニット蛋白質からなる膜蛋白質複合体（約２５万）ダイマー

X-ray structures of cytochrome bc1.

X-ray structure of fully oxidized bovine heart cytochrome coxidase.

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１３サブユニット蛋白質からなる膜蛋白質複合体（約２0万）ダイマー

The dimeric bovine complex is viewed
perpendicular to its 2-fold axis and parallel tothe membrane with the matrix below.

The yeast enzyme in complex withcytochrome c and the inhibitor
stigmatellin viewed with a ~90°
rotation about its 2-fold axis.

X-Ray structure of fully oxidized bovine heart cytochrome c oxidase.
The complex as viewed from the topPage 826

The proton-translocating channels in bovine complex IV

Voet Biochemistry 3e© 2004 John Wiley & Sons, Inc.

Voet Biochemistry 3e© 2004 John Wiley & Sons, Inc.

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SdhA

SdhB
SdhD

SdhC

The intricacies of complex II

Figur e 18-9

complex I2

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Complexes I, III, IV from bovine heart(blue, complex I; red, complex III; green, complex IV) and cytochrome c (black)

Figur e 9-22

Figur e 18-12

Page 608

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Page 827abc

Interpretive drawings of the mitochondrial membrane at various
stages of dissection.

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

F型ATPaseモーターの構造4

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F型ATPaseβ α βααδ

γb2εc10-12aElectron microscopy–based image of E. coli F1F0–ATPase.

X-Ray structure of F1–ATPase from bovine heart mitochondria.

X-Ray structure of F1–ATPase from bovine heart mitochondria.
The surface of the inner portion of the a3b3 assembly.

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The g,d, and esubunits in the X-ray structure of bovine F1–ATPase.

Electron density map of the yeast mitochondrial F1–c10 complex.

NMR structures of the c subunit of E. coli F1F0–ATPase.

Electron cryomicroscopy to obtain structures for rotational states of
the V-ATPase from the yeast S. cerevisiae.

Nature 521, 241–245 (14 May 2015)

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Interpolation between the three observed
rotational states of the V-ATPase.
The resulting series of structures showsten proteolipid subunits in the c-ring,setting the ATP:H + ratio for proton
pumping by the V-ATPase at 3:10, andreveals long and highly tilted
transmembrane α-helices in the a-subunitthat interact with the c-ring. The threedifferent maps reveal the conformationalchanges that occur to couple rotation in
the symmetry-mismatched soluble
catalytic region to the membrane-boundproton-translocating region. Almost all of
the subunits of the enzyme undergo
conformational changes during thetransitions between these three rotational
states. The structures of these states
provide direct evidence that deformation
during rotation enables the smoothtransmission of power through rotary
ATPases.

The Nobel Prize in Chemistry 1997

Paul D. Boyer

John E. Walker

Energy-dependent binding change mechanism for ATP synthesis byproton-translocating ATP synthase.

ATPaseの構造変化と触媒活性モデル

Jens C. Skou

The Nobel Prize in Chemistry 1997 was divided, one half jointly to Paul D. Boyer andJohn E. Walker "for their elucidation of the enzymatic mechanism underlying thesynthesis of adenosine triphosphate (ATP)" and the other half to Jens C. Skou "forthe first discovery of an ion-transporting enzyme, Na +, K+ -ATPase".

O(オープン）型：触媒不活性で基質・生成物に親和性なし
Ｌ(ルーズ）型：弱い親和性をもつが、触媒活性なし
Ｔ(タイト）型：強い親和性をもち、触媒活性をもつ

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Rotation of the c-ring in E. coli F 1F 0–ATPase

F型ATPase回転実証の実験系
回転蛍光標識した
アクチン繊維アビジン・ビオチンのスペーサー

ADP＋Pi
加水分解
ATP
ATPaseのα β γ複合体

Noji et al. (1997) NaturePage 833

Stepwise rotation of the gsubunit of F1 relative to an
immobilized a3 b3 unit at low ATP concentration.

Rotation of the c-ring in E. coli F1F0–ATPase. (b) The rotation ofa 3.6-mm-long actin filament in the presence of 5 mM MgATP.

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