Molecular models of the structural arrangement of subunits and the mechanism of proton translocation in the membrane domain of F(1)F(0) ATP synthase (Q33933696)

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English	Molecular models of the structural arrangement of subunits and the mechanism of proton translocation in the membrane domain of F(1)F(0) ATP synthase	scientific article

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scholarly article

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Europe PubMed Central

30 July 2017

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Europe PubMed Central

Molecular models of the structural arrangement of subunits and the mechanism of proton translocation in the membrane domain of F(1)F(0) ATP synthase (English)

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Europe PubMed Central

30 July 2017

author name string

G Groth

1

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Europe PubMed Central

30 July 2017

language of work or name

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publication date

1 May 2000

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Europe PubMed Central

30 July 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

30 July 2017

1458

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Europe PubMed Central

30 July 2017

2-3

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Europe PubMed Central

30 July 2017

417-427

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Europe PubMed Central

30 July 2017

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

1 reference

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7 January 2021

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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7 January 2021

Intersubunit rotation in active F-ATPase

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7 January 2021

Direct observation of the rotation of F1-ATPase

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7 January 2021

Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

1 reference

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7 January 2021

Chloroplast F0F1ATP Synthase Imaged by Atomic Force Microscopy

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

Model of the c-subunit oligomer in the membrane domain of F-ATPases.

1 reference

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7 January 2021

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

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7 January 2021

Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis.

1 reference

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7 January 2021

Energy transduction in ATP synthase

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7 January 2021

The motor of the ATP synthase.

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7 January 2021

The proton conducting F0-part of bacterial ATP synthases

1 reference

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7 January 2021

Secondary and tertiary structure of membrane proteins involved in proton translocation

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7 January 2021

The UNC operon nucleotide sequence, regulation and structure of ATP-synthase

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Prediction of transmembrane topology of F0 proteins from Escherichia coli F1F0 ATP synthase using variational and hydrophobic moment analyses.

1 reference

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7 January 2021

The transmembrane topology of the a [corrected] subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a.

1 reference

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7 January 2021

Topology of subunit a of the Escherichia coli ATP synthase

1 reference

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase

1 reference

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7 January 2021

Zero-length crosslinking between subunits delta and I of the H(+)-translocating ATPase of chloroplasts

1 reference

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7 January 2021

Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit b dimer.

1 reference

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7 January 2021

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://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

1 reference

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7 January 2021

Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.

1 reference

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7 January 2021

The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained

1 reference

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7 January 2021

Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

1 reference

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7 January 2021

The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900091-8

7 January 2021

Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

1 reference

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7 January 2021

Second-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structure

1 reference

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7 January 2021

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase

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7 January 2021

Disulfide bond formation in proteins

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Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis

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7 January 2021

Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli.

1 reference

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7 January 2021

Orientation of subunit c of the ATP synthase of Escherichia coli--a study with peptide-specific antibodies

1 reference

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7 January 2021

Organization of the F0 sector of Escherichia coli H+-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane

1 reference

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7 January 2021

Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1.

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7 January 2021

Changing the ion binding specificity of the Escherichia coli H(+)-transporting ATP synthase by directed mutagenesis of subunit c.

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7 January 2021

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.

1 reference

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7 January 2021

Effects of carbon source on expression of F0 genes and on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli

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7 January 2021

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10.1016/S0005-2728(00)00091-8

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Europe PubMed Central

30 July 2017

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Europe PubMed Central

30 July 2017

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