Evidence map›Paper›PMID 39260698›Full record

ArticleThe Journal of biological chemistry2024

Role of ammonia-lyases in the synthesis of the dithiomethylamine ligand during [FeFe]-hydrogenase maturation.

Adrien Pagnier, Batuhan Balci, Eric M Shepard, Hao Yang, Alex Drena, Gemma L Holliday, Brian M Hoffman, William E Broderick, Joan B Broderick

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. In vitro maturation of fully active [FeFe]-hydrogenase in a defined system including the iron carrier NfuA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Enhanced Stability ofPolymers · 2025
    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

9 authors.

Adrien PagnierDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.
Batuhan BalciDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.
Eric M ShepardDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.
Hao YangDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Alex DrenaDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Gemma L HollidayDigitisation, Pharmaceutical Science, Biopharmaceuticals R&D, AstraZeneca, Macclesfield, United Kingdom.
Brian M HoffmanDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
William E BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.
Joan B BroderickDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA. Electronic address: jbroderick@montana.edu.

Funding

Coboglobins-Cobalt-Substituted Hemoglobins and MyoglobinR01GM111097 · NIGMS · NORTHWESTERN UNIVERSITY · PI HOFFMAN, BRIAN M · 2014 to 2025
$6.7M
NIGMS NIH HHS R01 GM111097
6 · The paper itself

Abstract

The generation of an active [FeFe]-hydrogenase requires the synthesis of a complex metal center, the H-cluster, by three dedicated maturases: the radical S-adenosyl-l-methionine (SAM) enzymes HydE and HydG, and the GTPase HydF. A key step of [FeFe]-hydrogenase maturation is the synthesis of the dithiomethylamine (DTMA) bridging ligand, a process recently shown to involve the aminomethyl-lipoyl-H-protein from the glycine cleavage system, whose methylamine group originates from serine and ammonium. Here we use functional assays together with electron paramagnetic resonance and electron-nuclear double resonance spectroscopies to show that serine or aspartate together with their respective ammonia-lyase enzymes can provide the nitrogen for DTMA biosynthesis during in vitro [FeFe]-hydrogenase maturation. We also report bioinformatic analysis of the hyd operon, revealing a strong association with genes encoding ammonia-lyases, suggesting important biochemical and metabolic connections. Together, our results provide evidence that ammonia-lyases play an important role in [FeFe]-hydrogenase maturation by delivering the ammonium required for dithiomethylamine ligand synthesis.

Indexed as

HydrogenaseIron-Sulfur ProteinsAmmonia-LyasesBacterial ProteinsElectron Spin Resonance SpectroscopyLigandsMethylaminesOperonAmmonia-LyasesBacterial ProteinsHydrogenaseiron hydrogenaseIron-Sulfur ProteinsLigandsMethylaminesammonia lyaseammoniumdithiomethylamine[FeFe]-hydrogenaseglycine cleavage systemGTPaseHydFhyd operon

Identifiers

PMID39260698
PMCPMC11736057

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Registered trials

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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.