Evidence map›Paper›PMID 41140912›Full record

ArticleNature catalysis2025

Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.

Ana Lago-Maciel, Jéssica C Soares, Jan Zarzycki, Charles J Buchanan, Tristan Reif-Trauttmansdorff, Frederik V Schmidt, Stefano Lometto, Nicole Paczia, Jan M Schuller, D Flemming Hansen and 5 more

Abstract read
In one paragraph

Article in Nature catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Minimal ATP-Independent NAngewandte Chemie (International ed. in English) · 2026
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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

15 authors.

Ana Lago-MacielMicrobial Metalloenzymes Research Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0001-5637-9935
Jéssica C SoaresDepartment of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID 0009-0004-8682-8374
Jan ZarzyckiDepartment of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0002-6307-6497
Charles J BuchananEvolutionary Biochemistry Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0002-1840-5706
Tristan Reif-TrauttmansdorffDepartment of Chemistry, Philipps-University Marburg, Marburg, Germany.
Frederik V SchmidtMicrobial Metalloenzymes Research Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0003-3075-6637
Stefano LomettoEvolutionary Biochemistry Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0009-0002-2522-4396
Nicole PacziaMetabolomics Core Facility, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0003-3859-8186
Jan M SchullerDepartment of Chemistry, Philipps-University Marburg, Marburg, Germany.
D Flemming HansenDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, UK.ORCID 0000-0003-0891-220X
Gabriella T HellerDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, UK.ORCID 0000-0002-5672-0467
Simone PrinzCentral Electron Microscopy Facility, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Georg K A HochbergEvolutionary Biochemistry Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0002-7155-0451
Antonio J PierikDepartment of Chemistry, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID 0000-0002-1509-6370
Johannes G RebeleinMicrobial Metalloenzymes Research Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0003-2560-716X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors controlling their activity and specificity. Here we present the molecular structure of the methylthio-alkane reductase, which reveals large metalloclusters, including the P-cluster and the [Fe

Indexed as

BiocatalysisCarbon cycleCryoelectron microscopyOxidoreductases

Identifiers

PMID41140912
PMCPMC12552129

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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.