Domains, specific residues and conformational states involved in hydride ion transfer and proton pumping by nicotinamide nucleotide transhydrogenase from Escherichia coli (Q47729738)

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scientific article published in June 1998

Language	Label	Description	Also known as
English	Domains, specific residues and conformational states involved in hydride ion transfer and proton pumping by nicotinamide nucleotide transhydrogenase from Escherichia coli	scientific article published in June 1998

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

1 reference

Europe PubMed Central

Domains, specific residues and conformational states involved in hydride ion transfer and proton pumping by nicotinamide nucleotide transhydrogenase from Escherichia coli (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

1 reference

based on heuristic

inferred from title

Escherichia coli

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based on heuristic

inferred from title

author name string

J Rydström

1

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

X Hu

2

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

O Fjellström

3

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

J Meuller

4

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

J Zhang

5

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

C Johansson

6

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

T Bizouarn

7

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

publication date

1 June 1998

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

Biochimica et Biophysica Acta

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

1365

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

1-2

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

10-16

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

Properties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

The proton-translocating nicotinamide adenine dinucleotide transhydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Molecular biology of nicotinamide nucleotide transhydrogenase--a unique proton pump.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Properties of the soluble polypeptide of the proton-translocating transhydrogenase from Rhodospirillum rubrum obtained by expression in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Conformational dynamics of a mobile loop in the NAD(H)-binding subunit of proton-translocating transhydrogenases from Rhodospirillum rubrum and Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Structural and catalytic properties of the expressed and purified NAD(H)- and NADP(H)-binding domains of proton-pumping transhydrogenase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

High cyclic transhydrogenase activity catalyzed by expressed and reconstituted nucleotide-binding domains of Rhodospirillum rubrum transhydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Proton-translocating nicotinamide nucleotide transhydrogenase. Reconstitution of the extramembranous nucleotide-binding domains

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Evidence that the transfer of hydride ion equivalents between nucleotides by proton-translocating transhydrogenase is direct

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Prediction and site-specific mutagenesis of residues in transmembrane alpha-helices of proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli and bovine heart mitochondria.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Organization in the membrane of the N-terminal proton-translocating domain of the beta subunit of the pyridine nucleotide transhydrogenase of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Membrane sectors of F- and V-type H+-transporting ATPases

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

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%2898%2900038-3

7 January 2021

Correlation between active form and dimeric structure of mitochondrial nicotinamide nucleotide transhydrogenase from beef heart

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Cross-linking and N-(1-pyrenyl)maleimide labeling of cysteine mutants of proton-pumping pyridine nucleotide transhydrogenase of Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Characterization of the interaction of NADH with proton pumping E. coli transhydrogenase reconstituted in the absence and in the presence of bacteriorhodopsin.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

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

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Three-dimensional structure prediction of the NAD binding site of proton-pumping transhydrogenase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Site-directed mutagenesis of tyrosine residues at nicotinamide nucleotide binding sites of Escherichia coli transhydrogenase.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Mutation of conserved residues in the NADP(H)-binding domain of the proton translocating pyridine nucleotide transhydrogenase of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2898%2900038-3

7 January 2021

Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell.

1 reference

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7 January 2021

Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants

1 reference

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7 January 2021

Oxidants as stimulators of signal transduction

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Effects of metal ions on the substrate-specificity and activity of proton-pumping nicotinamide nucleotide transhydrogenase from Escherichia coli.

1 reference

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7 January 2021

Identifiers

10.1016/S0005-2728(98)00038-3

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/9693716

ResearchGate publication ID

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