Evidence map›Paper›PMID 34603675›Full record

ArticleChemical science2021

A chromophore-supported structural and functional model of dinuclear copper enzymes, for facilitating mechanism of action studies.

Qiu-Cheng Chen, Natalia Fridman, Boris Tumanskii, Zeev Gross

Abstract read
In one paragraph

Article in Chemical science, 2021. 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. Atomically Precise Clusterzymes: A Programmable Optoelectronic Platform for Neuroscience.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Review
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

4 authors.

Qiu-Cheng ChenSchulich Faculty of Chemistry, Technion-Israel Institute of Technology Haifa 32000 Israel chr10zg@technion.ac.il.ORCID https://orcid.org/0000-0001-5113-4832
Natalia FridmanSchulich Faculty of Chemistry, Technion-Israel Institute of Technology Haifa 32000 Israel chr10zg@technion.ac.il.
Boris TumanskiiSchulich Faculty of Chemistry, Technion-Israel Institute of Technology Haifa 32000 Israel chr10zg@technion.ac.il.
Zeev GrossSchulich Faculty of Chemistry, Technion-Israel Institute of Technology Haifa 32000 Israel chr10zg@technion.ac.il.ORCID https://orcid.org/0000-0003-1170-2115

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type III dicopper centres are the heart of the reactive sites of enzymes that catalyze the oxidation of catechols. Numerous synthetic model complexes have been prepared to uncover the fundamental chemistry involved in these processes, but progress is still lagging much behind that for heme enzymes. One reason is that the latter gain very much from the informative spectroscopic features of their porphyrin-based metal-chelating ligand. We now introduce sapphyrin-chelated dicopper complexes and show that they may be isolated in different oxidation states and coordination geometries, with distinctive colors and electronic spectra due to the heme-like ligands. The dicopper(i) complex

Identifiers

PMID34603675
PMCPMC8480325

What OpenQuestion holds

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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.