Evidence map›Paper›PMID 42333988›Full record

ArticleDalton transactions (Cambridge, England : 2003)2026

Direct electrochemistry as a mechanistic tool for studying engineered myoglobins: implications on carbene transferase activity.

Evelina Venckute, Amanda G Jarvis, Patricia Rodríguez-Maciá

Abstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 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

3 authors.

Evelina VenckuteEaStCHEM School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Amanda.Jarvis@ed.ac.uk.ORCID http://orcid.org/0009-0000-3619-938X
Amanda G JarvisEaStCHEM School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, UK. Amanda.Jarvis@ed.ac.uk.ORCID http://orcid.org/0000-0002-6414-0497
Patricia Rodríguez-MaciáSchool of Chemistry and Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK. prm28@leicester.ac.uk.ORCID http://orcid.org/0000-0003-3513-0115

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Direct electrochemistry tools offer exclusive insight into the redox properties of metalloenzymes. However, they have not found widespread use within the artificial enzyme community, despite their potential to help inform catalyst design. Herein, we describe the use of a simple and robust method for non-covalent immobilisation of a library of myoglobin-based (Mb) engineered and cofactor-substituted metalloenzymes onto carbon electrodes. This allowed the determination of the reduction potentials (

Identifiers

PMID42333988
PMCPMC13288710

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.