Evidence map›Paper›PMID 33004835›Full record

ArticleScientific reports2020

Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace.

Søren Brander, Istvan Horvath, Johan Ø Ipsen, Ausra Peciulyte, Lisbeth Olsson, Cristina Hernández-Rollán, Morten H H Nørholm, Susanne Mossin, Leila Lo Leggio, Corinna Probst and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.0field-weighted citation impact, top 4% of its field
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

28 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Histidine-Copper Site Variability in UiO-66: Monitoring Synthetic Intricacy with EPR Spectroscopy.Chemistry of materials : a publication of the American Chemical Society · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Journal of fungi (Basel, Switzerland) · 2025
    Article
  10. Article
  11. From Catalysis of Evolution to Evolution of Catalysis.Accounts of chemical research · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

12 authors at 4 institutions in 3 countries.

Søren BranderDepartment of Geoscience and Natural Resource Management, University of Copenhagen, 1958, Frederiksberg, Denmark.
Istvan HorvathDivision of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Kemivägen 10, 412 96, Gothenburg, Sweden.
Johan Ø IpsenDepartment of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark.
Ausra PeciulyteDivision of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, Kemivägen 10, 412 96, Gothenburg, Sweden.
Lisbeth OlssonDivision of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, Kemivägen 10, 412 96, Gothenburg, Sweden.
Cristina Hernández-RollánNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800, Kgs. Lyngby, Denmark.
Morten H H NørholmNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800, Kgs. Lyngby, Denmark.
Susanne MossinCentre for Catalysis and Sustainable Chemistry, Department of Chemistry, Technical University of Denmark, 2800, Kgs. Lyngby, Denmark.
Leila Lo LeggioDepartment of Chemistry, University of Copenhagen, 2100, Copenhagen Ø, Denmark.
Corinna ProbstDepartment of Biochemistry, Pharmacology and Cancer Biology and Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, NC, 27710, USA.
Dennis J ThieleDepartment of Biochemistry, Pharmacology and Cancer Biology and Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, NC, 27710, USA.
Katja S JohansenDepartment of Geoscience and Natural Resource Management, University of Copenhagen, 1958, Frederiksberg, Denmark. ksj@ign.ku.dk.
Chalmers University of Technology · SETechnical University of Denmark · DKUniversity of Copenhagen · DKDuke University · US

Funding

Metal Homeostasis in YeastR01GM041840 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALSPAUGH, ANDREW · 1989 to 2022
$6.5M
NIGMS NIH HHS R01 GM041840
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenase (LPMO) and copper binding protein CopC share a similar mononuclear copper site. This site is defined by an N-terminal histidine and a second internal histidine side chain in a configuration called the histidine brace. To understand better the determinants of reactivity, the biochemical and structural properties of a well-described cellulose-specific LPMO from Thermoascus aurantiacus (TaAA9A) is compared with that of CopC from Pseudomonas fluorescens (PfCopC) and with the LPMO-like protein Bim1 from Cryptococcus neoformans. PfCopC is not reduced by ascorbate but is a very strong Cu(II) chelator due to residues that interacts with the N-terminus. This first biochemical characterization of Bim1 shows that it is not redox active, but very sensitive to H

Indexed as

Models, MolecularCopperEscherichia coliHistidineHydrogen PeroxideMagnetic Resonance SpectroscopyOxidation-ReductionOxygenasesCopperHistidineHydrogen PeroxideOxygenases

Identifiers

PMID33004835
PMCPMC7529816
OpenAlexW3090986610

What OpenQuestion 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 OpenQuestion graph.