(Q27641401)

English

Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation

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scholarly article

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Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation (English)

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author name string

Avtar Singh

1

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Jamie D Venning

2

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Philip G Quirk

3

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Gijs I van Boxel

4

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Daniel J Rodrigues

5

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Scott A White

6

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J Baz Jackson

7

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language of work or name

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publication date

29 August 2003

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Journal of Biological Chemistry

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278

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35

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33208-16

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Physiological roles of nicotinamide nucleotide transhydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Crystal structures of transhydrogenase domain I with and without bound NADH

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Crystal structure of transhydrogenase domain III at 1.2 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Structure and mechanism of proton-translocating transhydrogenase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

28 Assay of nicotinamide nucleotide transhydrogenases in mammalian, bacterial, and reconstituted systems

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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/10.1074%2FJBC.M303061200

21 January 2018

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/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

The relation between the soluble factor associated with H(+)-transhydrogenase of Rhodospirillum rubrum and the enzyme from mitochondria and Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

A highly automated heavy-atom search procedure for macromolecular structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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/10.1074%2FJBC.M303061200

21 January 2018

Fast hydride transfer in proton-translocating transhydrogenase revealed in a rapid mixing continuous flow device

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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/10.1074%2FJBC.M303061200

21 January 2018

Use of chemical shifts in macromolecular structure determination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Stopped-flow kinetics of hydride transfer between nucleotides by recombinant domains of proton-translocating transhydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Stereochemistry of hydrogen-transfer in the energy-linked pyridine nucleotide transhydrogenase and related reactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Evidence for the stabilization of NADPH relative to NADP(+) on the dIII components of proton-translocating transhydrogenases from Homo sapiens and from Rhodospirillum rubrum by measurement of tryptophan fluorescence

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

Estimation of the H+/H− ratio of the reaction catalysed by the nicotinamide nucleotide transhydrogenase in chromatophores from over-expressing strains of Rhodospirillum rubrum and in liposomes inlaid with the purified bovine enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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/10.1074%2FJBC.M303061200

21 January 2018

Stopped-flow reaction kinetics of recombinant components of proton-translocating transhydrogenase with physiological nucleotides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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

https://api.crossref.org/works/10.1074%2FJBC.M303061200

21 January 2018

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10.1074/JBC.M303061200

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