Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer (Q73529490)

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scientific article published on 01 July 1997

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English	Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer	scientific article published on 01 July 1997

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4 November 2019

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

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4 November 2019

Rhodospirillum rubrum

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Rhodospirillum rubrum

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T Bizouarn

1

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R Grimley

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C Diggle

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C M Thomas

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J B Jackson

5

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1 July 1997

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Biochimica et Biophysica Acta

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1320

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3

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265-274

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4 November 2019

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

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

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.

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

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

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

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Inhibition of proton-translocating transhydrogenase from photosynthetic bacteria by N,N'-dicyclohexylcarbodiimide

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

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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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Mammalian membrane-bound adenylyl cyclases

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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

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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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

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TOWARD THE ISOLATION OF A PHOTOCHEMICAL REACTION CENTER IN RHODOPSEUDOMONAS SPHEROIDES

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The coupling between protonmotive force and the NAD(P)+ transhydrogenase in chromatophores from photosynthetic bacteria

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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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Utilization of conical equilibrium dialysis cells to shorten equilibration time

1 reference

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

1 reference

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Identifiers

10.1016/S0005-2728(97)00030-3

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9230921%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

1 reference

Europe PubMed Central

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4 November 2019

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