Evidence map›Paper›PMID 40827684›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Promiscuity in Molecular Mimics of the Cysteine Dioxygenase: Effects of Selenium in the Substrate and Cobalt as the Central Metal Ion.

Kilian Weißer, Edgar T K Weber, Gunasekaran Velmurugan, Beatrice Cula, Konstantin B Krause, Siad Wolff, M Qadri E Mubarak, Peter Comba, Sam P de Visser, Christian Limberg

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

10 authors.

Kilian WeißerInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.
Edgar T K WeberInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.
Gunasekaran VelmuruganInstitut für Anorganische Chemie and Interdisciplinary Center for Scientific Computing (IWR), Universität Heidelberg, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.
Beatrice CulaInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.
Konstantin B KrauseInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.
Siad WolffInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.ORCID 0000-0001-7927-8002
M Qadri E MubarakManchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Peter CombaInstitut für Anorganische Chemie and Interdisciplinary Center for Scientific Computing (IWR), Universität Heidelberg, Im Neuenheimer Feld 270, 69120, Heidelberg, Germany.
Sam P de VisserManchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Christian LimbergInstitut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Straße 2, 12489, Berlin, Germany.ORCID 0000-0002-0751-1386

Funding

Bioinspired Oxidation Catalysis with Iron Complexes Me1313/18-1/445916766Deutsche Forschungsgemeinschaft
6 · The paper itself

Abstract

Cysteine dioxygenase (CDO) catalyzes the conversion of cysteine with dioxygen to yield cysteine sulfinic acid, which lies at the branching point of cysteine catabolism. Despite many years of research there are still many questions related to its functioning. Thus, CDO is inactive with selenocysteine (Sec) or when the central iron ion is replaced by cobalt. In this context, we report here biomimetic CDO models with bound selenocysteamine substrate ligands, namely [Tp

Indexed as

Biomimetic MaterialsCobaltCysteine DioxygenaseSeleniumIonsMolecular StructureCobaltCysteine DioxygenaseIonsSeleniumCysteine dioxygenaseDioxygenase modelNonheme iron enzymesO2 activationSelenium

Identifiers

PMID40827684
PMCPMC12462750

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 Socratic graph.