The organization of the membrane domain and its interaction with the NADP(H)-binding site in proton-translocating transhydrogenase from E. coli (Q34807378)

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English	The organization of the membrane domain and its interaction with the NADP(H)-binding site in proton-translocating transhydrogenase from E. coli	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

4 August 2017

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Europe PubMed Central

The organization of the membrane domain and its interaction with the NADP(H)-binding site in proton-translocating transhydrogenase from E. coli (English)

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Europe PubMed Central

PubMed publication ID

4 August 2017

Escherichia coli

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author name string

Tania Bizouarn

1

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Europe PubMed Central

PubMed publication ID

4 August 2017

Magnus Althage

2

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Europe PubMed Central

PubMed publication ID

4 August 2017

Anders Pedersen

3

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Europe PubMed Central

PubMed publication ID

4 August 2017

Anna Tigerström

4

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Europe PubMed Central

PubMed publication ID

4 August 2017

Jenny Karlsson

5

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Europe PubMed Central

PubMed publication ID

4 August 2017

Carina Johansson

6

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4 August 2017

Jan Rydström

7

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4 August 2017

language of work or name

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publication date

1 September 2002

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Europe PubMed Central

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4 August 2017

Biochimica et Biophysica Acta

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4 August 2017

1555

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Europe PubMed Central

PubMed publication ID

4 August 2017

1-3

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Europe PubMed Central

PubMed publication ID

4 August 2017

122-127

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Europe PubMed Central

PubMed publication ID

4 August 2017

Physiological roles of nicotinamide nucleotide transhydrogenase

1 reference

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7 January 2021

Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria

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Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides

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7 January 2021

Molecular architecture of the rotary motor in ATP synthase

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7 January 2021

Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates.

1 reference

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7 January 2021

Crystal structure of transhydrogenase domain III at 1.2 A resolution

1 reference

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7 January 2021

The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria

1 reference

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7 January 2021

The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase

1 reference

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7 January 2021

Sequential assignment and secondary structure analysis of the NADP(H)-binding domain of Escherichia coli transhydrogenase

1 reference

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7 January 2021

NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: sequential assignment and global fold

1 reference

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7 January 2021

Interactions of the NADP(H)-binding domain III of proton-translocating transhydrogenase from escherichia coli with NADP(H) and the NAD(H)-binding domain I studied by NMR and site-directed mutagenesis

1 reference

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7 January 2021

Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy

1 reference

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7 January 2021

Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum

1 reference

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7 January 2021

The alternating site, binding change mechanism for proton translocation by transhydrogenase.

1 reference

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7 January 2021

Structure and mechanism of proton-translocating transhydrogenase.

1 reference

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7 January 2021

The heterotrimer of the membrane-peripheral components of transhydrogenase and the alternating-site mechanism of proton translocation.

1 reference

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7 January 2021

The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labeling

1 reference

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7 January 2021

The transmembrane domain and the proton channel in proton-pumping transhydrogenases

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2802%2900266-9

7 January 2021

Crosslinking between alpha and beta subunits defines the orientation and spatial relationship of some of the transmembrane helices of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2802%2900266-9

7 January 2021

Intersubunit crosslinking of the heterotetrameric proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli defines intersubunit contacts between transmembrane helices of the beta subunits

1 reference

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7 January 2021

Properties of a proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli with alpha and beta subunits linked through fused transmembrane helices

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7 January 2021

Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase

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7 January 2021

Assembly of multimeric proteins. Effect of mutations in the alpha-subunit on membrane assembly and activity of pyridine nucleotide transhydrogenase

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7 January 2021

Involvement of histidine-91 of the beta subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli.

1 reference

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7 January 2021

Characterization of mutants of beta histidine91, beta aspartate213, and beta asparagine222, possible components of the energy transduction pathway of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli

1 reference

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7 January 2021

The presence of an aqueous cavity in the proton-pumping pathway of the pyridine nucleotide transhydrogenase of Escherichia coli is suggested by the reaction of the enzyme with sulfhydryl inhibitors

1 reference

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7 January 2021

Identification of a region involved in the communication between the NADP(H) binding domain and the membrane domain in proton pumping E. coli transhydrogenase

1 reference

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7 January 2021

Identification of an aspartic acid residue in the beta subunit which is essential for catalysis and proton pumping by transhydrogenase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2802%2900266-9

7 January 2021

A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release

1 reference

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7 January 2021

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10.1016/S0005-2728(02)00266-9

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Europe PubMed Central

PubMed publication ID

4 August 2017

release_t6kx6gao6fal3j4gxiyddshi3m

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24 November 2022

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4 August 2017

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