(Q38290024)

1 September 2017

Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly (English)

1 reference

1 September 2017

Takayuki Ariga

1

1 reference

1 September 2017

Tomoko Masaike

series ordinal

2

1 reference

1 September 2017

Hiroyuki Noji

series ordinal

3

1 reference

1 September 2017

Masasuke Yoshida

series ordinal

4

1 reference

1 September 2017

language of work or name

English

0 references

publication date

18 April 2002

1 reference

Journal of Biological Chemistry

1 September 2017

1 reference

1 September 2017

277

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1 September 2017

28

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1 September 2017

24870-24874

1 reference

Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism

1 September 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Catalytic site forms and controls in ATP synthase catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

The rotary binding change mechanism of ATP synthases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

On what makes the gamma subunit spin during ATP hydrolysis by F(1).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Expression of the wild-type and the Cys-/Trp-less alpha 3 beta 3 gamma complex of thermophilic F1-ATPase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Catalytic site occupancy during ATP synthase catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

A rotary molecular motor that can work at near 100% efficiency

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Bi-site catalysis in F1-ATPase: does it exist?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Substitution of betaGlu(201) in the alpha(3)beta(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Monogenic causes of X-linked mental retardation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Why is the mechanical efficiency of F(1)-ATPase so high?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

Reverse engineering a protein: the mechanochemistry of ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202582200

21 January 2018

Identifiers

DOI

10.1074/JBC.M202582200

1 reference

1 September 2017

1 reference