(Q43028906)

English

Essential arginine residue of the F(o)-a subunit in F(o)F(1)-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F(o) proton channel

scientific article published in August 2010

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Essential arginine residue of the F(o)-a subunit in F(o)F(1)-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F(o) proton channel (English)

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

author name string

Noriyo Mitome

1

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Sakurako Ono

2

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Hiroki Sato

3

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Toshiharu Suzuki

4

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Nobuhito Sone

5

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Masasuke Yoshida

6

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Europe PubMed Central

PubMed publication ID

12 November 2017

language of work or name

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publication date

1 August 2010

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Europe PubMed Central

PubMed publication ID

12 November 2017

Biochemical Journal

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Europe PubMed Central

PubMed publication ID

12 November 2017

430

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Europe PubMed Central

PubMed publication ID

12 November 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

171-177

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

The ATP synthase--a splendid molecular machine

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Thermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

A new solution structure of ATP synthase subunit c from thermophilic Bacillus PS3, suggesting a local conformational change for H+-translocation

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Insertion scanning mutagenesis of subunit a of the F1F0 ATP synthase near His245 and implications on gating of the proton channel

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

ATP synthase: an electrochemical transducer with rotatory mechanics

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Energy transduction in ATP synthase

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase

1 reference

https://api.crossref.org/works/10.1042%2FBJ20100621

21 January 2018

Identifiers

10.1042/BJ20100621

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

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