Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation (Q30429196)

1 October 2017

Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation (English)

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1 October 2017

1 reference

Mizuki Sekiya

1

1 reference

1 October 2017

Hiroyuki Hosokawa

2

1 reference

1 October 2017

Mayumi Nakanishi-Matsui

3

1 reference

1 October 2017

Marwan K Al-Shawi

4

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1 October 2017

Robert K Nakamoto

5

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1 October 2017

Masamitsu Futai

6

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1 October 2017

language of work or name

English

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publication date

25 October 2010

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Journal of Biological Chemistry

1 October 2017

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1 October 2017

285

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1 October 2017

53

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1 October 2017

42058-42067

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The mechanism of rotating proton pumping ATPases

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

The rotary mechanism of the ATP synthase.

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

How azide inhibits ATP hydrolysis by the F-ATPases.

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Pause and rotation of F(1)-ATPase during catalysis

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Conformation of the gamma subunit at the gamma-epsilon-c interface in the complete Escherichia coli F(1)-ATPase complex by site-directed spin labeling

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

The rotary mechanism of ATP synthase

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Molecular architecture of the rotary motor in ATP synthase

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

The ATP synthase--a splendid molecular machine

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Catalytic mechanism of F1-ATPase

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Direct observation of the rotation of F1-ATPase

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration.

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3009931

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

14 July 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Effects of mutations in the beta subunit hinge domain on ATP synthase F1 sector rotation: interaction between Ser 174 and Ile 163.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Effect of epsilon subunit on the rotation of thermophilic Bacillus F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.176701

Escherichia coli ATP synthase alpha subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the steady state

21 January 2018

1 reference

12 December 2020

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

1 reference

12 December 2020

Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1074/JBC.M110.176701

1 reference

1 October 2017

1 reference

1 October 2017

PubMed publication ID

20974856

1 reference