Evidence map›Paper›PMID 26139605›Full record

ArticleThe Journal of biological chemistry2015

Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure.

Julius K Demmer, Haiyan Huang, Shuning Wang, Ulrike Demmer, Rudolf K Thauer, Ulrich Ermler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Article
  3. An electron-bifurcating "plug" to a protein nanowire in tungsten-dependent aldehyde detoxification.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Rapid-reaction kinetics of the bifurcating NADThe Journal of biological chemistry · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Julius K DemmerFrom the Max-Planck-Institut für Biophysik, D-60438 Frankfurt am Main, Germany and the Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany.
Haiyan Huangthe Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany.
Shuning Wangthe Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany.
Ulrike DemmerFrom the Max-Planck-Institut für Biophysik, D-60438 Frankfurt am Main, Germany and.
Rudolf K Thauerthe Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany thauer@mpi-marburg.mpg.de.
Ulrich ErmlerFrom the Max-Planck-Institut für Biophysik, D-60438 Frankfurt am Main, Germany and ulrich.ermler@biophys.mpg.de.
Max Planck Institute for Terrestrial Microbiology · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADH-dependent reduced ferredoxin:NADP oxidoreductase (NfnAB) is found in the cytoplasm of various anaerobic bacteria and archaea. The enzyme reversibly catalyzes the endergonic reduction of ferredoxin with NADPH driven by the exergonic transhydrogenation from NADPH onto NAD(+). Coupling is most probably accomplished via the mechanism of flavin-based electron bifurcation. To understand this process on a structural basis, we heterologously produced the NfnAB complex of Thermotoga maritima in Escherichia coli, provided kinetic evidence for its bifurcating behavior, and determined its x-ray structure in the absence and presence of NADH. The structure of NfnAB reveals an electron transfer route including the FAD (a-FAD), the [2Fe-2S] cluster of NfnA and the FAD (b-FAD), and the two [4Fe-4S] clusters of NfnB. Ferredoxin is presumably docked onto NfnB close to the [4Fe-4S] cluster distal to b-FAD. NAD(H) binds to a-FAD and NADP(H) consequently to b-FAD, which is positioned in the center of the NfnAB complex and the site of electron bifurcation. Arg(187) is hydrogen-bonded to N5 and O4 of the bifurcating b-FAD and might play a key role in adjusting a low redox potential of the FADH(•)/FAD pair required for ferredoxin reduction. A mechanism of FAD-coupled electron bifurcation by NfnAB is proposed.

Indexed as

Bacterial ProteinsBinding SitesCrystallography, X-RayElectronsElectron TransportElectrophoresis, Polyacrylamide GelFerredoxin-NADP ReductaseFerredoxinsFlavinsHydrogen BondingIron-Sulfur ProteinsModels, MolecularMultiprotein ComplexesNADOxidation-ReductionProtein BindingBacterial ProteinsFerredoxin-NADP ReductaseFerredoxinsFlavinsIron-Sulfur ProteinsMultiprotein ComplexesNADRecombinant Proteinscrystal structureelectron bifurcationenergy metabolismenzyme catalysisflaviniron-sulfur proteinNADH-dependent reduced ferredoxin-NADP oxidoreductase

Identifiers

PMID26139605
PMCPMC4571952
OpenAlexW1768003754

What OpenQuestion holds

Textmetadata
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.