Evidence map›Paper›PMID 35712785›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022

Selective Oxidations Using a Cytochrome P450 Enzyme Variant Driven with Surrogate Oxygen Donors and Light.

Joel H Z Lee, Matthew N Podgorski, Michael Moir, Alecia R Gee, Stephen G Bell

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 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

5 authors.

Joel H Z LeeDepartment of Chemistry, University of Adelaide, Adelaide, SA 5005, Australia.ORCID http://orcid.org/0000-0001-6288-9034
Matthew N PodgorskiDepartment of Chemistry, University of Adelaide, Adelaide, SA 5005, Australia.ORCID http://orcid.org/0000-0003-3238-8735
Michael MoirNational Deuteration Facility, Australian Nuclear Science and Technology Organisation (ANSTO), Lucas Heights, Sydney, NSW 2232, Australia.ORCID http://orcid.org/0000-0003-1684-3160
Alecia R GeeDepartment of Chemistry, University of Adelaide, Adelaide, SA 5005, Australia.ORCID http://orcid.org/0000-0001-8034-2817
Stephen G BellDepartment of Chemistry, University of Adelaide, Adelaide, SA 5005, Australia.ORCID http://orcid.org/0000-0002-7457-9727

Funding

Australian Nuclear Science and Technology Organisation 9152Australian Research Council DP200102411Commonwealth Scientific and Industrial Research Organisation Synthetic Biology Future Science Platform
6 · The paper itself

Abstract

Cytochrome P450 monooxygenase enzymes are versatile catalysts, which have been adapted for multiple applications in chemical synthesis. Mutation of a highly conserved active site threonine to a glutamate can convert these enzymes into peroxygenases that utilise hydrogen peroxide (H

Indexed as

Hydrogen PeroxideOxygenCytochrome P-450 Enzyme SystemKineticsOxidation-ReductionCytochrome P-450 Enzyme SystemHydrogen PeroxideOxygenbiocatalysisheme enzymesmonooxygenasesperoxygenasesprotein engineering

Identifiers

PMID35712785
PMCPMC9541349

What OpenQuestion holds

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LicenceCC BY-NC
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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.