Evidence map›Paper›PMID 27923678›Full record

ArticleFree radical biology & medicine2017

Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.

Aaron P Landry, Yiming Wang, Zishuo Cheng, Robert B Crochet, Yong-Hwan Lee, Huangen Ding

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2017. 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
2.1field-weighted citation impact, top 13% 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, 37 citations in OpenAlex.

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  16. The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  17. Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

6 authors at 1 institution in 1 country.

Aaron P LandryDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Yiming WangDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Zishuo ChengDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Robert B CrochetDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Yong-Hwan LeeDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
Huangen DingDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. Electronic address: hding@lsu.edu.
Louisiana State University · US

Funding

Modification of human mitoNEET [2Fe-2S] cluster under nitric oxide stressR15GM109399 · NIGMS · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI DING, HUANGEN · 2014 to 2014
$336k
NIGMS NIH HHS R15 GM109399
6 · The paper itself

Abstract

MitoNEET, a primary target of type II diabetes drug pioglitazone, has an essential role in regulating energy metabolism, iron homeostasis, and production of reactive oxygen species in mitochondria. Structurally, mitoNEET is anchored to the mitochondrial outer membrane via its N-terminal transmembrane α-helix. The C-terminal cytosolic domain of mitoNEET hosts a redox active [2Fe-2S] cluster via three cysteine and one histidine residues. Here we report that the reduced flavin nucleotides can rapidly reduce the mitoNEET [2Fe-2S] clusters under anaerobic or aerobic conditions. In the presence of NADH and flavin reductase, 1 molecule of flavin nucleotide is sufficient to reduce about 100 molecules of the mitoNEET [2Fe-2S] clusters in 4min under aerobic conditions. The electron paramagnetic resonance (EPR) measurements show that flavin mononucleotide (FMN), but not flavin adenine dinucleotide (FAD), has a specific interaction with mitoNEET. Molecular docking models further reveal that flavin mononucleotide binds mitoNEET at the region between the N-terminal transmembrane α-helix and the [2Fe-2S] cluster binding domain. The closest distance between the [2Fe-2S] cluster and the bound flavin mononucleotide in mitoNEET is about 10Å, which could facilitate rapid electron transfer from the reduced flavin nucleotide to the [2Fe-2S] cluster in mitoNEET. The results suggest that flavin nucleotides may act as electron shuttles to reduce the mitoNEET [2Fe-2S] clusters and regulate mitochondrial functions in human cells.

Indexed as

Energy MetabolismCysteineDiabetes Mellitus, Type 2DinitrocresolsElectron TransportHumansIronIron-Sulfur ProteinsMitochondrial ProteinsMolecular Docking SimulationNADNucleotidesOxidoreductasesPioglitazoneProtein BindingReactive Oxygen Species4,6-dinitro-o-cresolCISD1 protein, humanCysteineDinitrocresolsIronIron-Sulfur ProteinsMitochondrial ProteinsNADNucleotidesOxidoreductasesPioglitazoneReactive Oxygen SpeciesThiazolidinedionesFlavin nucleotidesIron-sulfur clustermitoNEETRedox regulationType II diabetes

Identifiers

PMID27923678
PMCPMC5209285
OpenAlexW2559270649

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.