H<sup>+</sup>‐ATPase: Catalysis and H<sup>+</sup>Translocation

Futai, Masamitsu; Iwamoto, Atsuko; Maeda, Masatomo

doi:10.1002/9783527615971.ch11

Cited by 13 publications

(17 citation statements)

References 112 publications

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“…3). One obvious di¡erence to the previous ¢ndings on TF 1 observed vigorous wobble movement of the ¢laments, which rotated one to two rounds in one and then in opposite direction. Even ¢lament moving in a continuous counter-clockwise rotation (Fig.…”

Section: The Characteristics Of Rotation Of Cf 1 -Qcontrasting

confidence: 69%

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

1999

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Rotation of the Q Q subunit in chloroplast F 1 -ATPase (CF 1 ) was investigated by using a single molecule observation technique, which is developed by Noji et al. to observe the rotation of a central Q Q subunit portion in the K K 3 L L 3 Q Q sub-complex of F 1 -ATPase from thermophilic Bacillus PS3 (TF 1 ) during ATP hydrolysis [Noji, H. et al. (1997) Nature 386, 299^302]. We used two cysteines of the Q Q subunit (Cys-199 and Cys-205) of CF 1 -ATPase, which are involved in the regulation of this enzyme, to fix the fluorochrome-labeled actin filament. Then we successfully observed a unidirectional, counter-clockwise rotation of the actin filament with the fluorescent microscope indicating the rotation of the Q Q subunit in CF 1 -ATPase. We conclude that the rotation of the Q Q subunit in the F 1 -motor is a ubiquitous phenomenon in all F 1 -ATPases in prokaryotes as well as in eukaryotes.z 1999 Federation of European Biochemical Societies.

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Section: The Characteristics Of Rotation Of Cf 1 -Qcontrasting

confidence: 69%

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

1999

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“…trans-membrane proton channel linking the proton-motive force of the membrane to the catalytic sites in F1. In all species examined F1 contains two major subunits, a and (, which together constitute -80%o by weight of F1 and three minor ones, fy, 6, and e (see Futai and Kanazawa, 1980). These proteins are probably assembled with a stoichiometry of 3ca:3(3: Iy: 1l: le (Catterall and Pedersen, 1971;Bragg and Hou, 1975;Fillingame, 1981).…”

Section: Introductionmentioning

confidence: 97%

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

Walker¹,

Saraste²,

Runswick³

et al. 1982

The EMBO Journal

5,083

3,296

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The a-and ,B-subunits of membrane-bound ATP synthase complex bind ATP and ADP: B contributes to catalyic sites, and a may be involved in regulation of ATP synthase activity. The sequences of ,B-subunits are highly conserved in Escherichia coli and bovine mitochondria. Also a and ( are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both a and (3 and in other enzymes that bind ATP or ADP in catalysis, notably myosin, phosphofructokinase, and adenylate kinase, help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.

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“…For the same reasons, sometimes multiplicities smaller than three may be found for nucleotide binding. Additional support for a total of six sites may be derived from the possibility of binding nucleotides to both isolated a and p subunits (review [25]) and from the established stoichiometry of m3/B3 (review [2]).…”

Section: Discussionmentioning

confidence: 99%

Total number and differentiation of nucleotide binding sites on mitochondrial F₁‐ATPase

Weber

Lücken

Schäfer

1985

European Journal of Biochemistry

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In this study 3'-0-[3-(4-azido-2-nitrophenyl)propionyl]-ADP was used as a photoaffinity analog for nucleotide binding sites on nucleotide-depleted F l-ATPase. Catalytic and binding properties of the labeled enzyme were investigated, The analog behaves as a competitive inhibitor in the dark (Ki = 50 pM). Photoirradiation of F1 in the presence of the analog leads to inactivation depending linearly on the incorporation of label. Complete inactivation is achieved at a stoichiometry of 3 mol/mol F1. The label is distributed between ct and fl subunits in a ratio of 30%: 70%. Although three sites were blocked covalently by photolabeling, three reversible sites of much higher affinity than the labeled sites were preserved. Mild alkaline treatment of photoinactivated enzyme leads to almost complete reactivation which is due to hydrolysis of the 3'-ester bond and release of the ADP moiety from the covalently bound analog. The conclusions drawn are as follows.1. The total number of sites which can be simultaneously occupied by nucleotides on F1 is six. azidonitrophenylpropionyl-ADP is a specific photolabel for the lower-affinity sites on nucleotide-depleted F This means that both types of sites can be differentiated by specific photoaffinity analogs. 3. The labeled low-affinity sites interact with the catalytic sites, abolishing enzyme turnover, when steadily occupied by ADP kept in place by the covalently linking residue, which by itself has no inhibitory effect on the enzyme.

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H⁺‐ATPase: Catalysis and H⁺Translocation

Cited by 13 publications

References 112 publications

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

Total number and differentiation of nucleotide binding sites on mitochondrial F₁‐ATPase

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H+‐ATPase: Catalysis and H+Translocation

Cited by 13 publications

References 112 publications

The γ subunit in chloroplast F1‐ATPase can rotate in a unidirectional and counter‐clockwise manner

The γ subunit in chloroplast F1‐ATPase can rotate in a unidirectional and counter‐clockwise manner

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

Total number and differentiation of nucleotide binding sites on mitochondrial F1‐ATPase

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About

H⁺‐ATPase: Catalysis and H⁺Translocation

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

The γ subunit in chloroplast F₁‐ATPase can rotate in a unidirectional and counter‐clockwise manner

Total number and differentiation of nucleotide binding sites on mitochondrial F₁‐ATPase