(Q39649790)

English

The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation

scientific article published on January 1995

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

13 September 2017

The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation (English)

1 reference

Europe PubMed Central

13 September 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

Bartl F

1

1 reference

Europe PubMed Central

13 September 2017

Deckers-Hebestreit G

2

1 reference

Europe PubMed Central

13 September 2017

Altendorf K

3

1 reference

Europe PubMed Central

13 September 2017

Zundel G

4

1 reference

Europe PubMed Central

13 September 2017

language of work or name

0 references

publication date

1 January 1995

1 reference

Europe PubMed Central

13 September 2017

number of pages

7

1 reference

based on heuristic

inferred from page(s)

Biophysical Journal

1 reference

Europe PubMed Central

13 September 2017

68

1 reference

Europe PubMed Central

13 September 2017

1

1 reference

Europe PubMed Central

13 September 2017

104-110

1 reference

Europe PubMed Central

13 September 2017

The role of arginine in the conserved polar loop of the c-subunit of the Escherichia coli H(+)-ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

ATP synthesis by oxidative phosphorylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

The mechanism of ATP synthase: a reassessment of the functions of the b and a subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

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=1281666

14 September 2017

Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Subunit c of F1F0 ATP synthase: structure and role in transmembrane energy transduction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Mutational analysis of the glycine-rich region of the c subunit of the Escherichia coli F0F1 ATPase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

The Fo complex of the proton-translocating F-type 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=1281666

14 September 2017

The proton conducting F0-part of bacterial ATP synthases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Structural Basis of Proton-Translocating Protein Function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

14 September 2017

Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Mutagenesis of the alpha subunit of the F1Fo-ATPase from Escherichia coli. Mutations at Glu-196, Pro-190, and Ser-199.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Influence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

Proton transfer and polarizability of hydrogen bonds in proteins coupled with conformational changes. I. Infrared investigation of poly(glutamic acid) with various N bases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

17 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

21 August 2018

The proton pore of the F0F1-ATPase of Escherichia coli: Ser-206 is not required for proton translocation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1281666

21 August 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP synthesis energized by delta pNa and delta psi in proteoliposomes containing the F0F1-ATPase from Propionigenium modestum

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ATP Synthetase (F1F0) of Escherichia coli K-12. High-Yield Preparation of Functional F0 by Hydrophobic Affinity Chromatography

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channel

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chemical modification of the F0 part of the ATP synthase (F1F0) from Escherichia coli. Effects on proton conduction and F1 binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modification of the F0 portion of the H+-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and effect on the proton channeling function

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments from subunit b

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/7711231

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/S0006-3495(95)80164-5

1 reference

Europe PubMed Central

13 September 2017

1 reference

Europe PubMed Central

13 September 2017

1 reference

Europe PubMed Central

13 September 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q39649790&oldid=1949339426"