Purification and properties of the F1F0 ATPase of Ilyobacter tartaricus, a sodium ion pump. (Q39566433)

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12 November 2019

title

Purification and properties of the F1F0 ATPase of Ilyobacter tartaricus, a sodium ion pump (English)

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12 November 2019

author name string

S Neumann

1

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12 November 2019

U Matthey

2

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12 November 2019

G Kaim

3

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12 November 2019

P Dimroth

4

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language of work or name

English

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publication date

1 July 1998

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12 November 2019

published in

Journal of Bacteriology

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12 November 2019

volume

180

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12 November 2019

page(s)

3312-3316

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12 November 2019

issue

13

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The ATP synthase--a splendid molecular machine

12 November 2019

cites work

1 reference

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Primary sodium ion translocating enzymes

14 September 2017

1 reference

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Studies on dissimilatory sulfate-reducing bacteria that decompose fatty acids. I. Isolation of new sulfate-reducing bacteria enriched with acetate from saline environments. Description of Desulfobacter postgatei gen. nov., sp. nov.

14 September 2017

1 reference

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Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump

14 September 2017

1 reference

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The F0F1-type ATP synthases of bacteria: structure and function of the F0 complex

14 September 2017

1 reference

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Catalytic mechanism of F1-ATPase

25 September 2017

1 reference

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Life by a new decarboxylation-dependent energy conservation mechanism with Na as coupling ion.

25 September 2017

1 reference

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Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107283

Subunit c from the sodium-ion-translocating F1F0-ATPase of Propionigenium modestum--production, purification and properties of the protein in dodecylsulfate solution.

17 June 2018

1 reference

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Purification of ATP synthase from Acetobacterium woodii and identification as a Na(+)-translocating F1F0-type enzyme.

17 June 2018

1 reference

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Characterization of the Na+-stimulated ATPase of Propionigenium modestum as an enzyme of the F1F0 type.

17 June 2018

1 reference

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Molecular basis for the coupling ion selectivity of F1F0 ATP synthases: probing the liganding groups for Na+ and Li+ in the c subunit of the ATP synthase from Propionigenium modestum.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107283

Formation of a functionally active sodium-translocating hybrid F1F0 ATPase in Escherichia coli by homologous recombination.

17 June 2018

1 reference

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The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=107283

A hybrid adenosinetriphosphatase composed of F1 of Escherichia coli and F0 of Propionigenium modestum is a functional sodium ion pump

21 August 2018

1 reference

12 December 2020

A triple mutation in the a subunit of the Escherichia coli/Propionigenium modestum F1Fo ATPase hybrid causes a switch from Na+ stimulation to Na+ inhibition

1 reference

12 December 2020

A double mutation in subunit c of the Na(+)-specific F1F0-ATPase of Propionigenium modestum results in a switch from Na+ to H(+)-coupled ATP synthesis in the Escherichia coli host cells

1 reference

12 December 2020

Specific protection by Na+ or Li+ of the F1F0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide

1 reference

12 December 2020

Kinetics of inactivation of the F1Fo ATPase of Propionigenium modestum by dicyclohexylcarbodiimide in relationship to H+ and Na+ concentration: probing the binding site for the coupling ions

1 reference

12 December 2020

10.1128/JB.180.13.3312-3316.1998

Identifiers

DOI

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12 November 2019

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