Evidence map›Paper›PMID 19561359›Full record

ArticleThe Journal of biological chemistry2009

The interaction of mitochondrial iron with manganese superoxide dismutase.

Amornrat Naranuntarat, Laran T Jensen, Samuel Pazicni, James E Penner-Hahn, Valeria C Culotta

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 64 citations in OpenAlex.

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  11. Prime Real Estate: Metals, Cofactors and MICOS.Frontiers in cell and developmental biology · 2022
    Review
  12. Review
  13. Article
  14. Article
  15. International journal of molecular sciences · 2020
    Review
  16. Article
  17. Article
  18. Article
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  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

5 authors at 2 institutions in 1 country.

Amornrat NaranuntaratDepartment of Environmental Health Sciences, Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205, USA.
Laran T Jensen
Samuel Pazicni
James E Penner-Hahn
Valeria C Culotta
Johns Hopkins University · USUniversity of Michigan–Ann Arbor · US

Funding

PILOT STUDY--ACID FOG, AN EXPERIMENTAL MODELP30ES003819 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI GROOPMAN, JOHN D · 1985 to 2012
$22.6M
Intracellular Pathways of Manganese TraffickingR01ES008996 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 1997 to 2012
$3.7M
STRUCTURAL INVESTIGATIONS OF METALLOPROTEIN METAL SITESR01GM038047 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PENNER-HAHN, JAMES E. · 1992 to 2008
$1.6M
STRUCTURAL INVESTIGATIONS OF METALLOPROTEIN METAL SITESR29GM038047 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PENNER-HAHN, JAMES E. · 1987 to 1991
–
NIEHS NIH HHS ES-08996NIEHS NIH HHS P30 ES003819NIEHS NIH HHS R01 ES008996NIGMS NIH HHS GM-38047NIGMS NIH HHS R01 GM038047
6 · The paper itself

Abstract

Superoxide dismutase 2 (SOD2) is one of the rare mitochondrial enzymes evolved to use manganese as a cofactor over the more abundant element iron. Although mitochondrial iron does not normally bind SOD2, iron will misincorporate into Saccharomyces cerevisiae Sod2p when cells are starved for manganese or when mitochondrial iron homeostasis is disrupted by mutations in yeast grx5, ssq1, and mtm1. We report here that such changes in mitochondrial manganese and iron similarly affect cofactor selection in a heterologously expressed Escherichia coli Mn-SOD, but not a highly homologous Fe-SOD. By x-ray absorption near edge structure and extended x-ray absorption fine structure analyses of isolated mitochondria, we find that misincorporation of iron into yeast Sod2p does not correlate with significant changes in the average oxidation state or coordination chemistry of bulk mitochondrial iron. Instead, small changes in mitochondrial iron are likely to promote iron-SOD2 interactions. Iron binds Sod2p in yeast mutants blocking late stages of iron-sulfur cluster biogenesis (grx5, ssq1, and atm1), but not in mutants defective in the upstream Isu proteins that serve as scaffolds for iron-sulfur biosynthesis. In fact, we observed a requirement for the Isu proteins in iron inactivation of yeast Sod2p. Sod2p activity was restored in mtm1 and grx5 mutants by depleting cells of Isu proteins or using a dominant negative Isu1p predicted to stabilize iron binding to Isu1p. In all cases where disruptions in iron homeostasis inactivated Sod2p, we observed an increase in mitochondrial Isu proteins. These studies indicate that the Isu proteins and the iron-sulfur pathway can donate iron to Sod2p.

Indexed as

Absorptiometry, PhotonATP-Binding Cassette TransportersGene Expression Regulation, FungalGlutaredoxinsHSP70 Heat-Shock ProteinsImmunoblottingIronMitochondriaMitochondrial ProteinsMutationProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuperoxide DismutaseSuperoxide Dismutase 2ATM1 protein, S cerevisiaeATP-Binding Cassette TransportersGlutaredoxinsGrx5 protein, S cerevisiaeHSP70 Heat-Shock ProteinsIronISU1 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae ProteinsSSQ1 protein, S cerevisiaeSuperoxide DismutaseSuperoxide Dismutase 2

Identifiers

PMID19561359
PMCPMC2755670
OpenAlexW1993779780

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.