A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme. (Q54502991)

30 May 2018

title

A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme. (English)

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30 May 2018

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Y Sambongi

1

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30 May 2018

I Ueda

series ordinal

2

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Y Wada

series ordinal

3

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M Futai

series ordinal

4

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publication date

1 October 2000

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Journal of Bioenergetics and Biomembranes

published in

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volume

32

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issue

5

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page(s)

441-448

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Rotation of Escherichia coli F(1)-ATPase

cites work

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12 December 2020

Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit

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12 December 2020

Structural changes linked to proton translocation by subunit c of the ATP synthase

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12 December 2020

ATP synthase: an electrochemical transducer with rotatory mechanics

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12 December 2020

F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)

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12 December 2020

Three-stepped rotation of subunits gamma and epsilon in single molecules of F-ATPase as revealed by polarized, confocal fluorometry

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12 December 2020

Interactions between the F1 and F0 parts in the Escherichia coli ATP synthase. Associations involving the loop region of C subunits.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

3'-O-(5-fluoro-2,4-dinitrophenyl)ADP ether and ATP ether. Affinity reagents for labeling ATPases.

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12 December 2020

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

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12 December 2020

The F0 complex of the Escherichia coli ATP synthase. Investigation by electron spectroscopic imaging and immunoelectron microscopy

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12 December 2020

Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide

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12 December 2020

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

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12 December 2020

The ATP synthase--a splendid molecular machine

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12 December 2020

Observations of rotation within the F(o)F(1)-ATP synthase: deciding between rotation of the F(o)c subunit ring and artifact

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12 December 2020

Effects of mutations of conserved Lys-155 and Thr-156 residues in the phosphate-binding glycine-rich sequence of the F1-ATPase beta subunit of Escherichia coli

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12 December 2020

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.

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12 December 2020

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

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12 December 2020

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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12 December 2020

Structural biology. Proton-powered turbine of a plant motor

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12 December 2020

Escherichia coli F1 ATPase is reversibly inhibited by intra- and intersubunit crosslinking: an approach to assess rotational catalysis.

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12 December 2020

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

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12 December 2020

Energy transduction in ATP synthase

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

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12 December 2020

A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis

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12 December 2020

F0F1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport

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12 December 2020

The alpha/beta subunit interaction in H(+)-ATPase (ATP synthase). An Escherichia coli alpha subunit mutation (Arg-alpha 296-->Cys) restores coupling efficiency to the deleterious beta subunit mutant (Ser-beta 174-->Phe).

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12 December 2020

Intersubunit rotation in active F-ATPase

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling

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12 December 2020

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

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12 December 2020

The gamma subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant gamma Met-23-->Lys.

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

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12 December 2020

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

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12 December 2020

Direct observation of the rotation of F1-ATPase

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12 December 2020

The glycine-rich sequence of the beta subunit of Escherichia coli H(+)-ATPase is important for activity

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12 December 2020

Molecular architecture of the rotary motor in ATP synthase

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Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.

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12 December 2020

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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Mechanisms of active transport in the FOF1 ATP synthase

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

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

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The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

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Identifiers

DOI

10.1023/A:1005656706248

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30 May 2018

Dimensions Publication ID

1013110599

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30 May 2018