Evidence map›Paper›PMID 18672901›Full record

ArticleBiochemistry2008

The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein.

Michael A Swanson, Robert J Usselman, Frank E Frerman, Gareth R Eaton, Sandra S Eaton

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Cryoelectron microscopy structure and mechanism of the membrane-associated electron-bifurcating flavoprotein Fix/EtfABCX.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. [A novel mutation in the ETFDH gene of an infant with multiple acyl-CoA dehydrogenase deficiency].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2018
    Article
  10. Article
  11. Article
  12. An electron-bifurcating caffeyl-CoA reductase.The Journal of biological chemistry · 2013
    Article
  13. Article
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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.

Michael A SwansonDepartment of Chemistry and Biochemistry, University of Denver, Denver, Colorado 80208, USA.
Robert J Usselman
Frank E Frerman
Gareth R Eaton
Sandra S Eaton
University of Colorado Denver · USUniversity of Denver · US

Funding

INTERACTION OF SPIN LABELS WITH TRANSITION METALSR01EB002807 · NIBIB · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI EATON, GARETH R · 2003 to 2008
$1.9M
NIBIB NIH HHS EB002807NIBIB NIH HHS R01 EB002807
6 · The paper itself

Abstract

Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) accepts electrons from electron transfer flavoprotein (ETF) and reduces ubiquinone from the ubiquinone pool. It contains one [4Fe-4S] (2+,1+) and one FAD, which are diamagnetic in the isolated oxidized enzyme and can be reduced to paramagnetic forms by enzymatic donors or dithionite. In the porcine protein, threonine 367 is hydrogen bonded to N1 and O2 of the flavin ring of the FAD. The analogous site in Rhodobacter sphaeroides ETF-QO is asparagine 338. Mutations N338T and N338A were introduced into the R. sphaeroides protein by site-directed mutagenesis to determine the impact of hydrogen bonding at this site on redox potentials and activity. The mutations did not alter the optical spectra, EPR g-values, spin-lattice relaxation rates, or the [4Fe-4S] (2+,1+) to FAD point-dipole interspin distances. The mutations had no impact on the reduction potential for the iron-sulfur cluster, which was monitored by changes in the continuous wave EPR signals of the [4Fe-4S] (+) at 15 K. For the FAD semiquinone, significantly different potentials were obtained by monitoring the titration at 100 or 293 K. Based on spectra at 293 K the N338T mutation shifted the first and second midpoint potentials for the FAD from +47 and -30 mV for wild type to -11 and -19 mV, respectively. The N338A mutation decreased the potentials to -37 and -49 mV. Lowering the midpoint potentials resulted in a decrease in the quinone reductase activity and negligible impact on disproportionation of ETF 1e (-) catalyzed by ETF-QO. These observations indicate that the FAD is involved in electron transfer to ubiquinone but not in electron transfer from ETF to ETF-QO. Therefore, the iron-sulfur cluster is the immediate acceptor from ETF.

Indexed as

AnimalsAsparagineCrystallography, X-RayElectron Spin Resonance SpectroscopyElectron-Transferring FlavoproteinsElectron TransportFlavin-Adenine DinucleotideHydrogen BondingIronIron-Sulfur ProteinsModels, MolecularMolecular StructureMutagenesis, Site-DirectedOxidoreductases Acting on CH-NH Group DonorsProtein Structure, SecondarySulfurAsparagineelectron-transferring-flavoprotein dehydrogenaseElectron-Transferring FlavoproteinsFlavin-Adenine DinucleotideIronIron-Sulfur ProteinsOxidoreductases Acting on CH-NH Group DonorsSulfurThreonine

Identifiers

PMID18672901
PMCPMC3106343
OpenAlexW2093476984

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.