Evidence map›Paper›PMID 41964152›Full record

ArticleAngewandte Chemie (International ed. in English)2026

Two-Dimensional Infrared Spectroscopy Reveals the Presence of a Bridging CO Ligand in Two Catalytic Intermediates of [FeFe] Hydrogenase.

Cornelius C M Bernitzky, Mathesh Vaithiyanathan, Manon T Lachmann, Igor V Sazanovich, Gregory M Greetham, Patricia Rodríguez-Maciá, James A Birrell, Marius Horch

Abstract read
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In one paragraph

Article in Angewandte Chemie (International ed. in English), 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

8 authors.

Cornelius C M BernitzkyDepartment of Physics, Ultrafast Dynamics in Catalysis, Freie Universität Berlin, Berlin, Germany.
Mathesh VaithiyanathanDepartment of Physics, Ultrafast Dynamics in Catalysis, Freie Universität Berlin, Berlin, Germany.
Manon T LachmannSchool of Chemistry and Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK.
Igor V SazanovichSTFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot, UK.
Gregory M GreethamSTFC Central Laser Facility, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot, UK.
Patricia Rodríguez-MaciáSchool of Chemistry and Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK.
James A BirrellSchool of Life Sciences, University of Essex, Colchester, UK.ORCID 0000-0002-0939-0573
Marius HorchDepartment of Physics, Ultrafast Dynamics in Catalysis, Freie Universität Berlin, Berlin, Germany.ORCID 0000-0001-6656-1749

Funding

Deutsche Forschungsgemeinschaft 2008 - 390540038Einstein Foundation BerlinRoyal Society RG∖R2∖232336Royal Society RGS∖R1∖231433Royal Society of Chemistry R22-2594924113Royal Society of Chemistry R23-6753486967STFC Central Laser Facility 23130006
6 · The paper itself

Abstract

[FeFe] hydrogenases are highly active, reversible enzymes for the interconversion of hydrogen with protons and electrons. Their active site H-cluster consists of a canonical [4Fe-4S] cluster covalently linked to a unique [2Fe]

Indexed as

Carbon MonoxideHydrogenaseIron-Sulfur ProteinsBiocatalysisCatalysisCatalytic DomainLigandsModels, MolecularSpectrophotometry, InfraredCarbon MonoxideHydrogenaseiron hydrogenaseIron-Sulfur ProteinsLigandscatalytic mechanismgreen hydrogenmetalloenzymeorganometallicvibrational spectroscopy

Identifiers

PMID41964152
PMCPMC13182199

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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.