Evidence map›Paper›PMID 42086585›Full record

ArticleNature communications2026

A mononuclear nonheme iron complex with higher affinity for O

Matthias Jux, Stefan Mebs, Michael Haumann, Sagie Katz, Ricardo Garcia-Serres, Peter Hildebrandt, Yong Wang, Wonwoo Nam, Kallol Ray

Abstract read
In one paragraph

Article in Nature communications, 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

9 authors.

Matthias JuxDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin, Germany.
Stefan MebsDepartment of Physics, Freie Universität Berlin, Berlin, Germany.
Michael HaumannDepartment of Physics, Freie Universität Berlin, Berlin, Germany.
Sagie KatzInstitute of Chemistry, Technische Universität Berlin, Berlin, Germany.
Ricardo Garcia-SerresLaboratoire Chimie et Biologie des Métaux, Grenoble, France.ORCID http://orcid.org/0000-0001-5203-0568
Peter HildebrandtInstitute of Chemistry, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0003-1030-5900
Yong WangInstitute of Drug Discovery Technology, Ningbo University, Ningbo, China.ORCID http://orcid.org/0000-0002-7668-2234
Wonwoo NamDepartment of Chemistry and Nano Science, Ewha Womans University, Seoul, South Korea. wwnam@ewha.ac.kr.ORCID http://orcid.org/0000-0001-8592-4867
Kallol RayDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin, Germany. kallol.ray@chemie.hu-berlin.de.ORCID http://orcid.org/0000-0003-2074-8844

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dioxygen activation at iron centers is central to many biological and synthetic oxidation processes. In proteins, the reactivity and stability of iron-dioxygen intermediates are often controlled by secondary-sphere interactions such as hydrogen bonding. For example, hemoglobin stabilizes a Fe-O

Identifiers

PMID42086585
PMCPMC13358151

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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.