Evidence map›Paper›PMID 27174986›Full record

ArticleScience (New York, N.Y.)2016

Radical SAM catalysis via an organometallic intermediate with an Fe-[5'-C]-deoxyadenosyl bond.

Masaki Horitani, Krista Shisler, William E Broderick, Rachel U Hutcheson, Kaitlin S Duschene, Amy R Marts, Brian M Hoffman, Joan B Broderick

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–field-weighted citation impact
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

69 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Mechanism of controlled radical initiation in radical SAM GTP 3',8-cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Iron-sulfur clusters: the road to room temperature.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  8. Review
  9. Review
  10. Chemical Antiquity in Metabolism.Accounts of chemical research · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Cluster-selectiveChemical science · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Unexpected diversity of dye-decolorizing peroxidases.Biochemistry and biophysics reports · 2023
    Article
  20. Review

9 more citing papers are in PubMed but not listed here.

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

8 authors.

Masaki HoritaniDepartment of Chemistry, Northwestern University, Evanston, IL 60208, USA.
Krista ShislerDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
William E BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Rachel U HutchesonDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Kaitlin S DuscheneDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Amy R MartsDepartment of Chemistry, Northwestern University, Evanston, IL 60208, USA.
Brian M HoffmanDepartment of Chemistry, Northwestern University, Evanston, IL 60208, USA. bmh@northwestern.edu jbroderick@chemistry.montana.edu.
Joan B BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA. bmh@northwestern.edu jbroderick@chemistry.montana.edu.

Funding

Coboglobins-Cobalt-Substituted Hemoglobins and MyoglobinR01GM111097 · NIGMS · NORTHWESTERN UNIVERSITY · PI HOFFMAN, BRIAN M · 2014 to 2025
$6.7M
Iron-Sulfur Clusters in Biological Radical GenerationR01GM054608 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI BRODERICK, JOAN B · 2001 to 2018
$4.7M
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE LYASE ACTIVASER29GM054608 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRODERICK, JOAN B. · 1997 to 2000
$102k
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE-LYASE ACTIVASER55GM054608 · NIGMS · AMHERST COLLEGE · PI BRODERICK, JOAN B. · 1996 to 1996
–
NIGMS NIH HHS GM 111097NIGMS NIH HHS GM 54608NIGMS NIH HHS R01 GM054608NIGMS NIH HHS R01 GM111097NIGMS NIH HHS R29 GM054608
6 · The paper itself

Abstract

Radical S-adenosylmethionine (SAM) enzymes use a [4Fe-4S] cluster to cleave SAM to initiate diverse radical reactions. These reactions are thought to involve the 5'-deoxyadenosyl radical intermediate, which has not yet been detected. We used rapid freeze-quenching to trap a catalytically competent intermediate in the reaction catalyzed by the radical SAM enzyme pyruvate formate-lyase activating enzyme. Characterization of the intermediate by electron paramagnetic resonance and (13)C, (57)Fe electron nuclear double-resonance spectroscopies reveals that it contains an organometallic center in which the 5' carbon of a SAM-derived deoxyadenosyl moiety forms a bond with the unique iron site of the [4Fe-4S] cluster. Discovery of this intermediate extends the list of enzymatic bioorganometallic centers to the radical SAM enzymes, the largest enzyme superfamily known, and reveals intriguing parallels to B12 radical enzymes.

Indexed as

BiocatalysisAcetyltransferasesElectron Spin Resonance SpectroscopyEnzymesIron-Sulfur ProteinsNuclear Magnetic Resonance, BiomolecularOrganometallic CompoundsS-AdenosylmethionineVitamin B 12AcetyltransferasesEnzymesIron-Sulfur ProteinsOrganometallic Compoundspyruvate formate-lyase activating enzymeS-AdenosylmethionineVitamin B 12

Identifiers

PMID27174986
PMCPMC4929858

What OpenQuestion holds

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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.