(Q30435062)

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Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell

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Europe PubMed Central

PMC publication ID

20 August 2017

Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell (English)

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Escherichia coli

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based on heuristic

inferred from title

author name string

Mizuki Sekiya

1

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Robert K Nakamoto

2

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Marwan K Al-Shawi

3

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Mayumi Nakanishi-Matsui

4

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Masamitsu Futai

5

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

language of work or name

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publication date

5 June 2009

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

284

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

33

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

22401-22410

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

The role of the betaDELSEED-loop of ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

The rotary mechanism of the ATP synthase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Temperature dependence of the rotation and hydrolysis activities of F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Determination of the partial reactions of rotational catalysis in F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

An alternative reaction pathway of F1-ATPase suggested by rotation without 80 degrees/40 degrees substeps of a sluggish mutant at low ATP

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

ATP-driven stepwise rotation of FoF1-ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Mechanically driven ATP synthesis by F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Mechanics of coupling proton movements to c-ring rotation in ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

The rotary mechanism of ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Rotational coupling in the F0F1 ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Energy transduction in the F1 motor of ATP synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

The ATP synthase--a splendid molecular machine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Catalytic mechanism of F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Direct observation of the rotation of F1-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

One-step purification of Escherichia coli H(+)-ATPase (F0F1) and its reconstitution into liposomes with neurotransmitter transporters

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

20 June 2018

Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.009019

21 January 2018

Highly coupled ATP synthesis by F1-ATPase single molecules

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.009019

21 January 2018

Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.009019

21 January 2018

ATP synthase F(1) sector rotation. Defective torque generation in the beta subunit Ser-174 to Phe mutant and its suppression by second mutations.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109.009019

21 January 2018

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.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2755962

26 November 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/19502237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Coupling factor F1 ATPase with defective beta subunit from a mutant of Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/19502237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli. Implications regarding the nature of energy coupling by F1-ATPases

1 reference

https://pubmed.ncbi.nlm.nih.gov/19502237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rotational catalysis of Escherichia coli ATP synthase F1 sector. Stochastic fluctuation and a key domain of the beta subunit

1 reference

https://pubmed.ncbi.nlm.nih.gov/19502237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/19502237

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M109.009019

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

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