Evidence map›Paper›PMID 28004877›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase.

William B O'Dell, Pratul K Agarwal, Flora Meilleur

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
13.9field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Review
  3. Electron transfer in polysaccharide monooxygenase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  6. Review
  7. Article
  8. Article
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  11. Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  12. Article
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  17. Review
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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 at 1 institution in 1 country.

William B O'DellDepartment of Molecular and Structural Biochemistry, North Carolina State University and Biology and Soft Matter Division, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, TN, 37831, USA.ORCID 0000-0002-8063-5190
Pratul K AgarwalDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville and Computational Biology Institute and Computer Science and Mathematics Division, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, TN, 37831, USA.
Flora MeilleurDepartment of Molecular and Structural Biochemistry, North Carolina State University and Biology and Soft Matter Division, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, TN, 37831, USA.ORCID 0000-0001-9313-8989
Oak Ridge National Laboratory · US

Funding

Conformational sub-states in enzyme catalysis: Applications to ribonucleaseR01GM105978 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AGARWAL, PRATUL K, CHENNUBHOTLA, SRINIVAS CHAKRA · 2014 to 2018
$2.8M
NIGMS NIH HHS R01 GM105978
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases have attracted vast attention owing to their abilities to disrupt glycosidic bonds via oxidation instead of hydrolysis and to enhance enzymatic digestion of recalcitrant substrates including chitin and cellulose. We have determined high-resolution X-ray crystal structures of an enzyme from Neurospora crassa in the resting state and of a copper(II) dioxo intermediate complex formed in the absence of substrate. X-ray crystal structures also revealed "pre-bound" molecular oxygen adjacent to the active site. An examination of protonation states enabled by neutron crystallography and density functional theory calculations identified a role for a conserved histidine in promoting oxygen activation. These results provide a new structural description of oxygen activation by substrate free lytic polysaccharide monooxygenases and provide insights that can be extended to reactivity in the enzyme-substrate complex.

Indexed as

Catalytic DomainMixed Function OxygenasesModels, MolecularNeurospora crassaOxygenPolysaccharidesMixed Function OxygenasesOxygenPolysaccharidescopperoxidoreductasesoxygen activationpolysaccharide monooxygenasesprotein structures

Identifiers

PMID28004877
PMCPMC5340418
OpenAlexW2561236934

What OpenQuestion holds

Textmetadata
LicenceTDM
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.