A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme (Q77363731)

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scientific article published on 01 April 1999

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English	A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme	scientific article published on 01 April 1999

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10216162%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

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

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10216162%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

Rhodospirillum rubrum

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Rhodospirillum rubrum

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S J Peake

1

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5 December 2019

J D Venning

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5 December 2019

J B Jackson

3

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5 December 2019

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1 April 1999

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5 December 2019

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Biochimica et Biophysica Acta

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5 December 2019

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5 December 2019

1

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5 December 2019

159-169

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5 December 2019

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

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Interdomain hydride transfer in proton-translocating transhydrogenase

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

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

1 reference

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

1 reference

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

1 reference

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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

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

1 reference

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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

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

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

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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

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

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7 January 2021

The cDNA sequence of proton-pumping nicotinamide nucleotide transhydrogenase from man and mouse

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Purification and properties of the H(+)-nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus

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7 January 2021

Nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus; the H+/H- ratio and the activation state of the enzyme during reduction of acetyl pyridine adenine dinucleotide

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7 January 2021

Studies on the mitochondrial energy-linked pyridine nucleotide transhydrogenase.

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7 January 2021

The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli.

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7 January 2021

Method for preparing NAD labeled with 3 H of high specific radioactivity in the 4-nicotinamide position

1 reference

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7 January 2021

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

1 reference

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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

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7 January 2021

Cyclic reactions catalysed by detergent-dispersed and reconstituted transhydrogenase from beef-heart mitochondria; implications for the mechanism of proton translocation.

1 reference

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7 January 2021

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

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7 January 2021

Identifiers

10.1016/S0005-2728(99)00013-4

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10216162%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10216162%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

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