A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release (Q32081556)

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

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scholarly article

1 reference

Europe PubMed Central

6 July 2017

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

1 reference

Europe PubMed Central

6 July 2017

author name string

D J Rodrigues

1

1 reference

Europe PubMed Central

6 July 2017

J D Venning

2

1 reference

Europe PubMed Central

6 July 2017

P G Quirk

3

1 reference

Europe PubMed Central

6 July 2017

J B Jackson

4

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Europe PubMed Central

6 July 2017

language of work or name

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publication date

1 March 2001

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Europe PubMed Central

6 July 2017

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Europe PubMed Central

6 July 2017

268

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Europe PubMed Central

6 July 2017

5

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Europe PubMed Central

6 July 2017

1430-1438

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Europe PubMed Central

6 July 2017

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Structure and mechanism of proton-translocating transhydrogenase.

1 reference

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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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Crystal structure of transhydrogenase domain III at 1.2 A resolution

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Interaction of nucleotides with the NAD(H)-binding domain of the proton-translocating transhydrogenase of Rhodospirillum rubrum.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

The binding of nucleotides to domain I proteins of the proton-translocating transhydrogenases from Rhodospirillum rubrum and Escherichia coli as measured by equilibrium dialysis.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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

1 reference

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Catalytic properties of hybrid complexes of the NAD(H)-binding and NADP(H)-binding domains of the proton-translocating transhydrogenases from Escherichia coli and Rhodospirillum rubrum.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

A shift in the equilibrium constant at the catalytic site of proton-translocating transhydrogenase: significance for a 'binding-change' mechanism

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Interdomain hydride transfer in proton-translocating transhydrogenase.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Toward understanding tryptophan fluorescence in proteins.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Letter to the Editor: Sequence-specific resonance assignments for the NADP(H)-binding component (domain III) of proton- translocating transhydrogenase from Rhodospisrillum rubrum

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Altered amino acid metabolism in lrp mutants of Escherichia coli K12 and their derivatives

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Mutation of Tyr235 in the NAD(H)-binding subunit of the proton-translocating nicotinamide nucleotide transhydrogenase of Rhodospirillum rubrum affects the conformational dynamics of a mobile loop and lowers the catalytic activity of the enzyme

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

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/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.02008.X

21 January 2018

Mapping of residues in the NADP(H)-binding site of proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. A study of structure and function

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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10.1046/J.1432-1327.2001.02008.X

1 reference

Europe PubMed Central

6 July 2017

1 reference

Europe PubMed Central

6 July 2017

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