Evidence map›Paper›PMID 30346729›Full record

ReviewAccounts of chemical research2018

Mechanism of Radical Initiation in the Radical S-Adenosyl-l-methionine Superfamily.

William E Broderick, Brian M Hoffman, Joan B Broderick

Open access · greenAbstract readReview
In one paragraph

Review in Accounts of chemical research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. 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
  6. Article
  7. Structural Basis for CbioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Cluster-selectiveChemical science · 2023
    Article
  17. An Artificial [FeJournal of the American Chemical Society · 2023
    Article
  18. Article
  19. Review
  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

3 authors at 2 institutions in 1 country.

William E BroderickDepartment of Chemistry and Biochemistry , Montana State University , Bozeman , Montana 59717 , United States.
Brian M HoffmanDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.ORCID 0000-0002-3100-0746
Joan B BroderickDepartment of Chemistry and Biochemistry , Montana State University , Bozeman , Montana 59717 , United States.ORCID 0000-0001-7057-9124
Montana State University · USNorthwestern University · US

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
Radical SAM Enzymes: Radical Mechanisms Central to BiologyR35GM131889 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI Joan B Broderick · 2019 to 2026
$3.0M
Generation and Repair of an Unusual UV PhotoproductR01GM067804 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI BRODERICK, JOAN B. · 2003 to 2006
$1.0M
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE LYASE ACTIVASER29GM054608 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRODERICK, JOAN B. · 1997 to 2000
$102k
NIGMS NIH HHS R01 GM054608NIGMS NIH HHS R01 GM067804NIGMS NIH HHS R01 GM111097NIGMS NIH HHS R29 GM054608NIGMS NIH HHS R35 GM131889
6 · The paper itself

Abstract

The seeds for recognition of the vast superfamily of radical S-adenosyl-l-methionine (SAM) enzymes were sown in the 1960s, when Joachim Knappe found that the dissimilation of pyruvate was dependent on SAM and Fe(II), and Barker and co-workers made similar observations for lysine 2,3-aminomutase. These intriguing observations, coupled with the evidence that SAM and Fe were cofactors in radical catalysis by these enzyme systems, drew us in the 1990s to explore how Fe(II) and SAM initiate radical reactions. Our early work focused on the same enzyme Knappe had originally characterized: the pyruvate formate-lyase activating enzyme (PFL-AE). Our discovery of an iron-sulfur cluster in this enzyme, together with similar findings for other SAM-dependent enzymes at the time, led to the recognition of an emerging class of enzymes that use iron-sulfur clusters to cleave SAM, liberating the 5'-deoxyadenosyl radical (5'-dAdo•) that initiates radical reactions. A major bioinformatics study by Heidi Sofia and co-workers identified the enzyme superfamily denoted Radical SAM, now known to span all kingdoms of life with more than 100,000 unique sequences encoding enzymes that catalyze remarkably diverse reactions. Despite the limited sequence similarity and vastly divergent reactions catalyzed, the radical SAM enzymes appear to employ a common mechanism for initiation of radical chemistry, a mechanism we have helped to clarify over the last 25 years. A reduced [4Fe-4S]

Indexed as

AcetyltransferasesElectron Spin Resonance SpectroscopyEnzymesFree RadicalsIron-Sulfur ProteinsS-AdenosylmethionineAcetyltransferasesEnzymesFree RadicalsIron-Sulfur Proteinspyruvate formate-lyase activating enzymeS-Adenosylmethionine

Identifiers

PMID30346729
PMCPMC6324848
OpenAlexW2898055507

What OpenQuestion holds

Textmetadata
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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.