A conformational change in the isolated NADP(H)-binding component (dIII) of transhydrogenase induced by low pH: a reflection of events during proton translocation by the complete enzyme? (Q44122013)

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English	A conformational change in the isolated NADP(H)-binding component (dIII) of transhydrogenase induced by low pH: a reflection of events during proton translocation by the complete enzyme?	scientific article

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scholarly article

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Europe PubMed Central

30 November 2017

A conformational change in the isolated NADP(H)-binding component (dIII) of transhydrogenase induced by low pH: a reflection of events during proton translocation by the complete enzyme? (English)

1 reference

Europe PubMed Central

30 November 2017

author name string

Daniel J Rodrigues

1

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Europe PubMed Central

30 November 2017

J Baz Jackson

2

1 reference

Europe PubMed Central

30 November 2017

publication date

1 September 2002

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Europe PubMed Central

30 November 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

30 November 2017

1555

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Europe PubMed Central

30 November 2017

1-3

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Europe PubMed Central

30 November 2017

8-13

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Europe PubMed Central

30 November 2017

Physiological roles of nicotinamide nucleotide transhydrogenase

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

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

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

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7 January 2021

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

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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

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7 January 2021

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

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

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

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The unusual transhydrogenase of Entamoeba histolytica

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

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7 January 2021

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

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Crystal structure of transhydrogenase domain III at 1.2 A resolution

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

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

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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

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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.

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

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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

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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

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Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding

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Resonance energy transfer between points in a reconstituted skeletal muscle thin filament. A conformational change of the thin filament in response to a change in Ca2+ concentration

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Resonance energy transfer: methods and applications

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

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7 January 2021

Site-directed mutagenesis of charged and potentially proton-carrying residues in the beta subunit of the proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli. Characterization of the beta H91, beta D392, and beta K424

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

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

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10.1016/S0005-2728(02)00247-5

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Europe PubMed Central

30 November 2017

release_ylwjlmb44zcxhmop2h7x2ofyta

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30 November 2017

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