Evidence map›Paper›PMID 41684659›Full record

ArticleChemical science2026

From two to one: resolving CO binding in acetyl-CoA synthase.

Denise Poire, Cornelius C M Bernitzky, Mathesh Vaithiyanathan, Berta M Martins, Christian Lorent, Tamanna M Ahamad, Vladimir Pelmenschikov, Igor Sazanovich, Gregory M Greetham, Ingo Zebger and 3 more

Abstract read
In one paragraph

Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Denise PoireFreie Universität Berlin, Department of Physics, Ultrafast Dynamics in Catalysis Arnimallee 14 14195 Berlin Germany marius.horch@fu-berlin.de.ORCID https://orcid.org/0009-0008-0278-3703
Cornelius C M BernitzkyFreie Universität Berlin, Department of Physics, Ultrafast Dynamics in Catalysis Arnimallee 14 14195 Berlin Germany marius.horch@fu-berlin.de.ORCID https://orcid.org/0009-0002-9548-5890
Mathesh VaithiyanathanFreie Universität Berlin, Department of Physics, Ultrafast Dynamics in Catalysis Arnimallee 14 14195 Berlin Germany marius.horch@fu-berlin.de.ORCID https://orcid.org/0009-0000-3082-8077
Berta M MartinsHumboldt-Universität zu Berlin, Department of Biology, Structural Biology/Biochemistry Unter den Linden 6 10099 Berlin Germany.ORCID https://orcid.org/0000-0001-9250-000X
Christian LorentTechnische Universität Berlin, Department of Chemistry, Spectroscopic Characterization of Metalloproteins Straße des 17. Juni 135 10623 Berlin Germany.ORCID https://orcid.org/0000-0001-9057-4523
Tamanna M AhamadTechnische Universität Berlin, Department of Chemistry, Spectroscopic Characterization of Metalloproteins Straße des 17. Juni 135 10623 Berlin Germany.ORCID https://orcid.org/0000-0003-1721-2758
Vladimir PelmenschikovTechnische Universität Berlin, Department of Chemistry, Modelling of Biomolecular Systems Straße des 17. Juni 135 10623 Berlin Germany.ORCID https://orcid.org/0000-0002-0523-4418
Igor SazanovichSTFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus Didcot OX11 0QX UK.ORCID https://orcid.org/0000-0002-8000-7645
Gregory M GreethamSTFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus Didcot OX11 0QX UK.
Ingo ZebgerTechnische Universität Berlin, Department of Chemistry, Spectroscopic Characterization of Metalloproteins Straße des 17. Juni 135 10623 Berlin Germany.ORCID https://orcid.org/0000-0002-6354-3585
Holger DobbekHumboldt-Universität zu Berlin, Department of Biology, Structural Biology/Biochemistry Unter den Linden 6 10099 Berlin Germany.ORCID https://orcid.org/0000-0002-4122-3898
Maria Andrea MroginskiTechnische Universität Berlin, Department of Chemistry, Modelling of Biomolecular Systems Straße des 17. Juni 135 10623 Berlin Germany.ORCID https://orcid.org/0000-0002-7497-5631
Marius HorchFreie Universität Berlin, Department of Physics, Ultrafast Dynamics in Catalysis Arnimallee 14 14195 Berlin Germany marius.horch@fu-berlin.de.ORCID https://orcid.org/0000-0001-6656-1749

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetyl-CoA synthase (ACS) catalyzes the condensation of acetyl-CoA from carbon monoxide (CO), a methyl group, and coenzyme A, enabling the fixation of CO into biomolecules. Recent low-temperature ENDOR studies proposed that the enzyme can bind two CO ligands in its reduced A

Identifiers

PMID41684659
PMCPMC12893122

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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.