Evidence map›Paper›PMID 18717593›Full record

ArticleBiochemistry2008

Thioredoxin reductase from Thermoplasma acidophilum: a new twist on redox regulation.

Hector H Hernandez, Orlando A Jaquez, Michael J Hamill, Sean J Elliott, Catherine L Drennan

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Thioredoxin targets fundamental processes in a methane-producing archaeon, Methanocaldococcus jannaschii.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Review
  12. Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism.Acta crystallographica. Section D, Biological crystallography · 2009
    Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Hector H HernandezDepartment of Chemistry, Massachusetts Institute of Technology, 16-573, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Orlando A Jaquez
Michael J Hamill
Sean J Elliott
Catherine L Drennan
Boston University · USMassachusetts Institute of Technology · US

Funding

Interdepartmental Biotechnology Training ProgramT32GM008334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WITTRUP, KARL DANE · 1989 to 2018
$15.2M
X-ray studies of metalloenzyme regulation and catalysisR01GM065337 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2002 to 2008
$1.8M
Structural Studies of Archaeal Ribonucleotide ReductasesF31GM073569 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HERNANDEZ, HECTOR H · 2004 to 2005
$87k
NIGMS NIH HHS F31 GM073569NIGMS NIH HHS GM65337NIGMS NIH HHS GM73569NIGMS NIH HHS R01 GM065337NIGMS NIH HHS T32 GM008334
6 · The paper itself

Abstract

Thioredoxin reductases (TrxRs) regulate the intracellular redox environment by using NADPH to provide reducing equivalents for thioredoxins (Trxs). Here we present the cloning and biochemical characterization of a putative TrxR (Ta0984) and a putative Trx (Ta0866) from Thermoplasma acidophilum. Our data identify Ta0866 as a Trx through its capacity to reduce insulin and be reduced by Escherichia coli TrxR in a NADPH-dependent manner. Our data also establish Ta0984 as a TrxR due to its ability to reduce T. acidophilum Trx ( taTrx), although not in a NADPH- or NADH-dependent manner. To explore the apparent inability of taTrxR to use NADPH or NADH as a reductant, we carried out a complete electrochemical characterization, which suggests that redox potential is not the source of this nonreactivity [Hamill et al. (2008) Biochemistry 47, 9738-9746]. Turning to crystallographic analysis, a 2.35 A resolution structure of taTrxR, also presented here, shows that despite the overall structural similarity to the well-characterized TrxR from E. coli (RMSD 1.30 A (2) for chain A), the "NADPH binding pocket" is not conserved. E. coli TrxR residues implicated in NADPH binding, H175, R176, R177, and R181, have been substituted with E185, Y186, M187, and M191 in the ta protein. Thus, we have identified a Trx and TrxR protein system from T. acidophilum for which the TrxR shares overall structural and redox properties with other TrxRs but lacks the appropriate binding motif to use the standard NADPH reductant. Our discovery of a TrxR that does not use NADPH provides a new twist in redox regulation.

Indexed as

Binding SitesCrystallography, X-RayKineticsModels, MolecularNADPOxidation-ReductionProtein Structure, TertiaryRecombinant ProteinsThermoplasmaThioredoxin-Disulfide ReductaseNADPRecombinant ProteinsThioredoxin-Disulfide Reductase

Identifiers

PMID18717593
PMCPMC2804746
OpenAlexW2078836434

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.