Evidence map›Paper›PMID 41784227›Full record

ArticleThe FEBS journal2026

Insights into the catalytic mechanism of formate dehydrogenases from different microbial sources.

Laura Legnani, Marco Gargiulo, Elia Lio, Enrico Mario Alessandro Fassi, Giovanni Grazioso, Maria Assunta Chiacchio, Barış Binay, Stefania Brocca, Francesco Secundo

Abstract read
In one paragraph

Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Laura LegnaniDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy.
Marco GargiuloIstituto di Scienze e Tecnologie Chimiche "Giulio Natta", CNR, Milan, Italy.
Elia LioIstituto di Scienze e Tecnologie Chimiche "Giulio Natta", CNR, Milan, Italy.
Enrico Mario Alessandro FassiDipartimento di Scienze Farmaceutiche, University of Milan, Milan, Italy.ORCID https://orcid.org/0000-0001-6282-4273
Giovanni GraziosoDipartimento di Scienze Farmaceutiche, University of Milan, Milan, Italy.
Maria Assunta ChiacchioDipartimento di Scienze del Farmaco e della Salute, University of Catania, Catania, Italy.
Barış BinayDepartment of Bioengineering, Gebze Technical University, Faculty of Engineering, Kocaeli, Türkiye.ORCID https://orcid.org/0000-0002-6190-6549
Stefania BroccaDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy.ORCID https://orcid.org/0000-0001-7256-4436
Francesco SecundoIstituto di Scienze e Tecnologie Chimiche "Giulio Natta", CNR, Milan, Italy.ORCID https://orcid.org/0000-0002-7052-9634

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Four formate dehydrogenases (FDHs) from Pseudomonas sp. 101, Myceliophthora thermophila, Chaetomium thermophilum, and Ogataea parapolymorpha were recombinantly produced, purified, and characterized to investigate their catalytic properties and reaction mechanisms. The enzymes were studied for their ability to oxidize formate to carbon dioxide (CO

Indexed as

Bacterial ProteinsFormate DehydrogenasesFungal ProteinsBiocatalysisCarbon DioxideCatalysisCatalytic DomainChaetomiumFormatesKineticsMolecular Dynamics SimulationNADOxidation-ReductionPseudomonasSordarialesSubstrate SpecificityBacterial ProteinsCarbon DioxideFormate DehydrogenasesFormatesformic acidFungal ProteinsNADFDH reaction mechanismformate oxidationhydride transferNAD+ reductionQM/MM calculations

Identifiers

PMID41784227
PMCPMC13440586

What OpenQuestion holds

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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.