Does the gamma subunit move to an abortive position of ATP hydrolysis when the F1.ADP.Mg complex isomerizes to the inactive F1*.ADP.Mg complex? (Q41252080)

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Language	Label	Description	Also known as
English	Does the gamma subunit move to an abortive position of ATP hydrolysis when the F1.ADP.Mg complex isomerizes to the inactive F1*.ADP.Mg complex?	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

28 September 2017

1 reference

Europe PubMed Central

Does the gamma subunit move to an abortive position of ATP hydrolysis when the F1.ADP.Mg complex isomerizes to the inactive F1*.ADP.Mg complex? (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

author name string

W S Allison

1

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

J M Jault

2

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

C Dou

3

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

N B Grodsky

4

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Europe PubMed Central

PubMed publication ID

28 September 2017

publication date

1 October 1996

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Europe PubMed Central

PubMed publication ID

28 September 2017

Journal of Bioenergetics and Biomembranes

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Europe PubMed Central

PubMed publication ID

28 September 2017

28

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Europe PubMed Central

PubMed publication ID

28 September 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

433-438

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Europe PubMed Central

PubMed publication ID

28 September 2017

A model for ATP hydrolysis catalysed by F1-ATPases based on kinetic and structural considerations

1 reference

https://api.crossref.org/works/10.1007%2FBF02113985

21 January 2018

Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with adenosine triphosphatase of bovine heart submitochondrial particles

1 reference

https://api.crossref.org/works/10.1007%2FBF02113985

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1007%2FBF02113985

21 January 2018

Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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Active/inactive state transitions of the chloroplast F1 ATPase are induced by a slow binding and release of Mg2+. Relationship to catalysis and control of F1 ATPases

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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The synthesis of enzyme-bound ATP by soluble chloroplast coupling factor 1

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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High affinity binding of monovalent Pi by beef heart mitochondrial adenosine triphosphatase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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Adenine nucleotide-binding sites on mitochondrial F1-ATPase: studies of the inactive complex formed upon binding ADP at a catalytic site

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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The alpha 3 beta 3 complex, the catalytic core of F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

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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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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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.

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

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inferred from PubMed ID database lookup

Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP.

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

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ATP synthesis catalyzed by the mitochondrial F1-F0 ATP synthase is not a reversal of its ATPase activity

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP.

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The reconstituted alpha 3 beta 3 delta complex of the thermostable F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

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The proton-translocating ATPase of Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

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Kinetics of ATP hydrolysis by F1-ATPase and the effects of anion activation, removal of tightly bound nucleotides, and partial inhibition of the ATPase by covalent modification

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Adenine nucleotide binding at a noncatalytic site of mitochondrial F1-ATPase accelerates a Mg(2+)- and ADP-dependent inactivation during ATP hydrolysis

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure and Mechanism of F0F1-Type ATP Synthases and ATPases

1 reference

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based on heuristic

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The binding change mechanism for ATP synthase--some probabilities and possibilities

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase.

1 reference

https://pubmed.ncbi.nlm.nih.gov/8951090

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1007/BF02113985

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 September 2017

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