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2 edition of proton-translocating transhydrogenase from Rhodospirillum rubrum found in the catalog.

proton-translocating transhydrogenase from Rhodospirillum rubrum

Ian James Cunningham

proton-translocating transhydrogenase from Rhodospirillum rubrum

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Published by University of Birmingham in Birmingham .
Written in English


Edition Notes

Thesis (Ph.D) - University of Birmingham, School of Biochemistry, 1992.

Statementby Ian James Cunningham.
ID Numbers
Open LibraryOL20860844M


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proton-translocating transhydrogenase from Rhodospirillum rubrum by Ian James Cunningham Download PDF EPUB FB2

Proton-Translocating Transhydrogenase From Rhodospirillum Rubrum Kinetic Analysis of the Reaction Catalysed by Recombinant, Nucleotide-Binding Domains Shows that Hydride Transfer Does Not Involve Intermediate Redox Reactions Transhydrogenase couples the transfer of reducing equivalents (hydride ion equivalents) between NAD(H) and NADP(H) to the translocation of protons across a membrane.

Proton-Translocating Transhydrogenase from Rhodospirillum rubrum: Hydride Transfer in   Properties of the soluble polypeptide of the proton-translocating transhydrogenase from Rhodospirillum rubrum obtained by expression in Escherichia coli.

Diggle C(1), Hutton M, Jones GR, Thomas CM, Jackson JB. Author information: (1)School of   The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.

Quirk PG(1), Smith KJ, Thomas CM, Jackson ://   proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains Tania Bizouarn, Shaun Stilwell, Jamie Venning, Nick P.J. Cotton, J. Baz Jackson) School of Biochemistry, Uni˝ersity of Birmingham, Edgbaston, Birmingham, B15 2TT, UK Transhydrogenase couples the translocation of protons across a membrane to the transfer of reducing equivalents between NAD(H) and NADP(H).

Using transhydrogenase from Rhodospirillum rubrum we have examined the pH dependences of the `forward' and `reverse' reactions, and of the `cyclic' reaction (NADP(H)-dependent reduction of the analogue, acetyl pyridine adenine dinucleotide, by NADH).

Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods.

This is the first description of the structure of dIII from a bacterial ://   Mutation of Tyr 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.

Diggle C(1), Quirk PG, Bizouarn T, Grimley RI, Cotton NP, Thomas CM, Jackson ://   Proton-translocating transhydrogenase (also known as nicotinamide nucleotide transhydrogenase (NNT)) is found in the plasma membranes of bacteria and the inner mitochondrial membranes of :// 1.

Introduction. The proton-translocating nicotinamide nucleotide transhydrogenase of Rhodospirillum rubrum couples the transfer of hydride ions between NAD(H) and NADP(H) to the vectorial pumping of protons across the bacterial cell membrane (for recent reviews see,), according to the equation: NADH+NADP + +H + OUT ⇔NAD + +NADPH+H + IN.

The enzyme has a tripartite structure   Abstract. The nicotinamide nucleotide transhydrogenase of bovine mitochondria is a homodimer of monomer M =The monomer is composed of three domains, an NH-terminal residue-long hydrophilic domain I that binds NAD(H), a central residue-long hydrophobic domain II that is largely membrane intercalated and carries the enzyme's proton channel, and a COOH-terminal The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides Transhydrogenase comprises three domains.

Domains I and III are peripheral to the membrane and possess the NAD(H)‐ and NADP(H)‐binding sites, respectively, and domain II spans the membrane. Domain III of transhydrogenase from Rhodospirillum rubrum was expressed at high levels in Escherichia coli, and :// Rhodospirillum rubrum NAD(P) transhydrogenase subunit alpha part 2 Add BLAST: Interaction i Subunit structure i.

Complex of an alpha and a beta chain; in Rhodospirillum, the alpha chain seems to be made of two subunits. 3.D the proton-translocating transhydrogenase (pth) family: Phylogenomic databases.

eggNOG i: The Rhodospirillum (Rsp.) rubrum transhydrogenase was the first to be shown to have a dissociable dI component, a finding that opened up a new approach in studies on the kinetics and the structure of the enzyme.

A complex of dI and dIII from Rsp. rubrum transhydrogenase catalyzes very fast hydride transfer from NADH to NADP +. The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides. kinetics of a lag phase at the onset of a “cyclic reaction” catalysed by complexes of the dI and dIII components of transhydrogenase from Rhodospirillum rubrum, and on the kinetics of fluorescence changes associated with nucleotide binding, reveal   Transhydrogenase catalyzes the reduction of NADP+ by NADH coupled to the translocation of protons across a membrane.

The polypeptide composition of the enzyme in Rhodospirillum rubrum is unique in that the NAD(H)-binding domain (called Ths) exists as a separate polypeptide.

Ths was expressed in Escherichia coli and :// proton-translocating NAD(P)+ transhydrogenase IUBMB Comments The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the ://?ecno= Williams R, Cotton N P J, Thomas C M, Jackson J B.

Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain-structure of the enzyme. Microbiology—UK. ; The Rhodospirillum (Rsp.) rubrum transhydrogenase was the first to be shown to have a dissociable dI component, a finding that opened up a new approach in studies on the kinetics and the structure Background: Transhydrogenase, located in the inner membranes of animal mitochondria and the cytoplasmic membranes of bacteria, couples the transfer of reducing equivalents between NAD(H) and NADP(H) to proton pumping.

The protein comprises three subunits termed dI, dII and dIII. The dII component spans the membrane. The dI component, which contains the binding site for NAD+/NADH, (00)   proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and e¡ects of bound nucleotides Philip G.

Quirk a;*, K. John Smith a, Christopher M. Thomas b, J. Baz Jackson a a School of Biochemistry, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK Results: We have solved the high-resolution crystal structure of a dI:dIII complex of transhydrogenase from Rhodospirillum rubrum—the first from a transhydrogenase of any is a heterotrimer, having two polypeptides of dI and one of dIII.

The dI polypeptides fold into a dimer. The loop on dIII, which binds the nicotinamide ring of NADP(H), is inserted into the NAD(H) binding cleft (01) Proton-translocating transhydrogenase is found in the inner membranes of animal mitochondria, and in the cytoplasmic membranes of many bacteria.

It catalyses hydride transfer from NADH to NADP AbstractTranshydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods.

This is the first description of the structure of dIII from a bacterial ://   Transhydrogenase couples the translocation of protons across a membrane to the transfer of reducing equivalents between NAD(H) and NADP(H). Using transhydrogenase from Rhodospirillum rubrum we have examined the pH dependences of the 'forward' and 'reverse' reactions, and of the 'cyclic' reaction (NADP(H)-dependent reduction of the analogue, acetyl pyridine adenine dinucleotide, by Abstract.

The Tyr residue in the mobile loop region of the soluble, domain I polypeptide (called Th s) of the proton-translocating transhydrogenase from Rhodospirillum rubrum has been substituted by Asn and by Phe.

The recombinant proteins were expressed at high levels in Escherichia coli and purified to homogeneity. The two well defined resonances at and ppm, observed in the one Rhodospirillum rubrum is a purple non-sulfur bacteria. It most easily is found in marine environments, which may range from ponds, to brackish ditches and even ://   MutationofTyrintheNAD(H)-bindingSubunitofthe Proton-translocatingNicotinamideNucleotideTranshydrogenaseof RhodospirillumrubrumAffectstheConformationalDynamicsofa Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum Article in Biochimica et Biophysica Acta () Proton-translocating transhydrogenase component 1.

Rhodospirillum rubrum (strain ATCC / ATH / DSM / LMG / NCIB / S1) NAD(P) transhydrogenase subunit alpha part 1 Add BLAST: Interaction i Subunit structure i.

Heterotrimer of two alpha chains and a beta (PntB) chain; in Rhodospirillum, the alpha chain is made Transhydrogenase, which catalyses the reduction of NADP⁺ by NADH coupled to proton translocation across a membrane, may be unique in the photosynthetic bacterium Rhodospirillum ://   Nicotinamide nucleotide transhydrogenase: a model for utilization of substrate binding energy for proton translocation.

A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction.

Proton-Translocating Transhydrogenase The genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum have been cloned using a probe constructed with the polymerase chain reaction, genomic   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.

Biochimica et Biophysica Acta (BBA) - Bioenergetics(1), DOI: /S(97) Abstract. The molecular masses of the purified, recombinant nucleotide-binding domains (domains I and III) of transhydrogenase from Rhodospirillum rubrum were determined by electrospray mass spectrometry.

The values obtained, 40, Da, for domains I and III, respectively, are similar to those estimated from the amino acid sequences of the The Phototrophic Prokaryotes.

Editors: Peschek, Günter A., Löffelhardt, Wolfgang, The Inorganic Pyrophosphate Synthase from Rhodospirillum Rubrum and its Gene. Pages Baltscheffsky, Margareta (et al.) Preview Buy Chap19 € Proton-Translocating Transhydrogenase From Rhodospirillum Rubrum.

Pages Venning, Jamie D  › Life Sciences › Animal Sciences. Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the enzyme.

Williams R, Cotton NP, Thomas CM, Jackson JB. Williams R, Cotton NPJ, Thomas CM and Jackson JB () Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the :// The genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum have been cloned using a probe constructed with the polymerase chain reaction, genomic DNA as target and oligonucleotide primers corresponding to amino acid sequence obtained from the purified soluble subunit.

There is a cluster of three genes, designated pntAA, pntAB and pntB, whose. Proton-translocating transhydrogenase (also known as nicotinamide nucleotide transhydrogenase (NNT)) is found in the plasma membranes of bacteria and the inner mitochondrial membranes of ://  Both bacteria and mitochrondria produce NADPH for amino acid biosynthesis and to remove reactive oxygen species.

The enzyme that makes NADPH must translocate a proton across the membrane and transfer a hydride from NADH to NADP+—processes that happen some 40 Å apart. To understand this complex geometry, Leung et al.

solved the structures of the entire transhydrogenase Jackson, J.B.: Mutation of Tyr 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 ://