Cross-linking of two beta subunits in the closed conformation in F1-ATPase (Q43026214)

12 November 2017

title

Cross-linking of two beta subunits in the closed conformation in F1-ATPase (English)

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12 November 2017

Tsunoda SP

1

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12 November 2017

Muneyuki E

2

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12 November 2017

Amano T

3

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12 November 2017

Yoshida M

4

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12 November 2017

Noji H

5

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12 November 2017

language of work or name

English

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publication date

1 February 1999

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Journal of Biological Chemistry

12 November 2017

published in

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12 November 2017

volume

274

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12 November 2017

issue

9

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12 November 2017

page(s)

5701-5706

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Coupling between catalytic sites and the proton channel in F1F0-type ATPases

12 November 2017

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21 January 2018

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Structural asymmetry of F1-ATPase caused by the gamma subunit generates a high affinity nucleotide binding site

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A single mutation at the catalytic site of TF1-alpha3beta3gamma complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity.

21 January 2018

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21 January 2018

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Analysis of time-dependent change of Escherichia coli Fl-ATPase activity and its relationship with apparent negative cooperativity

21 January 2018

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Catalytic activities of alpha3beta3gamma complexes of F1-ATPase with 1, 2, or 3 incompetent catalytic sites

21 January 2018

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

21 January 2018

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

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Direct observation of the rotation of F1-ATPase

21 January 2018

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Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site

21 January 2018

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Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite

21 January 2018

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Characteristics of the combination of inhibitory magnesium and azide with the F1 ATPase from chloroplasts

21 January 2018

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Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition

21 January 2018

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Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics

21 January 2018

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The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site

21 January 2018

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Mutations in the nucleotide binding domain of the alpha subunits of the F1-ATPase from thermophilic Bacillus PS3 that affect cross-talk between nucleotide binding sites

21 January 2018

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Inhibition and inactivation of the F1 adenosinetriphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide

21 January 2018

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Effects of inducing expression of cloned genes for the F0 proton channel of the Escherichia coli F1F0 ATPase

21 January 2018

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34 Preparation and properties of complex V

21 January 2018

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A New Model of Proton Motive ATP Synthesis: Acid-Base Cluster Hypothesis

21 January 2018

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The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites

21 January 2018

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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.

21 January 2018

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Unisite catalysis without rotation of the gamma-epsilon domain in Escherichia coli F1-ATPase

21 January 2018

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

21 January 2018

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21 January 2018

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Nucleotide-depleted beef heart F1-ATPase exhibits strong positive catalytic cooperativity

21 January 2018

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Kinetic analysis of proton translocation catalyzed by F0F1 ATPase

21 January 2018

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Inhibitory effect of NaN3 on the F0F1 ATPase of submitochondrial particles as related to nucleotide binding

21 January 2018

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The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.9.5701

1 reference

release_hoxlxlbnkbggzgn2tcv3q7udte

12 November 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/hoxlxlbnkbggzgn2tcv3q7udte

mapped directly with Wikidata item

24 November 2022

based on heuristic

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