Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation (Q33933640)

30 July 2017

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title

Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation (English)

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30 July 2017

M Futai

1

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30 July 2017

H Omote

series ordinal

2

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30 July 2017

Y Sambongi

series ordinal

3

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30 July 2017

Y Wada

series ordinal

4

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30 July 2017

language of work or name

English

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publication date

1 May 2000

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Biochimica et Biophysica Acta

30 July 2017

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30 July 2017

1458

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30 July 2017

2-3

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30 July 2017

276-288

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ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches

30 July 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Catalytic mechanism of F1-ATPase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Membrane sectors of F- and V-type H+-transporting ATPases

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The ATP synthase--a splendid molecular machine

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Mechanisms of active transport in the FOF1 ATP synthase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

ATP synthase: an electrochemical transducer with rotatory mechanics

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Intersubunit rotation in active F-ATPase

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Functional and idling rotatory motion within F1-ATPase

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Direct observation of the rotation of F1-ATPase

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

ATP synthase. Conditions under which all catalytic sites of the F1 moiety are kinetically equivalent in hydrolyzing ATP

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The alpha subunit of ATP synthase (F0F1): the Lys-175 and Thr-176 residues in the conserved sequence (Gly-X-X-X-X-Gly-Lys-Thr/Ser) are located in the domain required for stable subunit-subunit interaction.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Nucleotide occupancy of F1-ATPase catalytic sites under crystallization conditions

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Beta-subunit of Escherichia coli F1-ATPase. An amino acid replacement within a conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

F1-ATPase, roles of three catalytic site residues

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Conserved Glu-181 and Arg-182 residues of Escherichia coli H(+)-ATPase (ATP synthase) beta subunit are essential for catalysis: properties of 33 mutants between beta Glu-161 and beta Lys-201 residues

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Escherichia coli H(+)-ATPase (ATP synthase): catalytic site and roles of subunit interactions in energy coupling.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Beta subunit Glu-185 of Escherichia coli H(+)-ATPase (ATP synthase) is an essential residue for cooperative catalysis.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Mutational replacements of conserved amino acid residues in the alpha subunit change the catalytic properties of Escherichia coli F1-ATPase.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Mutations in alpha-subunit of Escherichia coli F1-ATPase obtained by hydroxylamine-mutagenesis of plasmids carrying the uncA gene

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Escherichia coli F0F1-ATPase. Residues involved in catalysis and coupling

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Temperature-sensitive Escherichia coli mutant with an altered initiation codon of the uncG gene for the H+-ATPase gamma subunit

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Alpha 3 beta 3 complex of thermophilic ATP synthase. Catalysis without the gamma-subunit

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Escherichia coli H+-ATPase: loss of the carboxyl terminal region of the gamma subunit causes defective assembly of the F1 portion

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Deletion of seven amino acid residues from the gamma subunit of Escherichia coli H+-ATPase causes total loss of F1 assembly on membranes.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Energy coupling, turnover, and stability of the F0F1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

The ATP synthase gamma subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Beta-gamma subunit interaction is required for catalysis by H(+)-ATPase (ATP synthase). Beta subunit amino acid replacements suppress a gamma subunit mutation having a long unrelated carboxyl terminus

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Conformational changes in the Escherichia coli ATP synthase (ECF1F0) monitored by nucleotide-dependent differences in the reactivity of Cys-87 of the gamma subunit in the mutant betaGlu-381 --> Ala.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Stability of the Escherichia coli ATP synthase F0F1 complex is dependent on interactions between gamma Gln-269 and the beta subunit loop beta Asp-301-beta Asp-305

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Direct observation of the rotation of epsilon subunit in F1-ATPase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

ATP synthase's second stalk comes into focus

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900080-3

10.1016/S0005-2728(00)00080-3

7 January 2021

Identifiers

DOI

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30 July 2017

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