Evidence map›Paper›PMID 28852004›Full record

ArticleScientific reports2017

Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.

Samuel L Freeman, Anne Martel, Emma L Raven, Gordon C K Roberts

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution.Protein science : a publication of the Protein Society · 2026
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  17. Solution structure of the cytochrome P450 reductase-cytochromeThe Journal of biological chemistry · 2018
    Article
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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

4 authors at 2 institutions in 2 countries.

Samuel L FreemanDepartment of Chemistry and Leicester Institute of Structural and Chemical Biology, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester, LE1 7RH, UK.ORCID 0000-0002-1467-5282
Anne MartelInstitut Laue-Langevin, 71 avenue des Martyrs, 38000, Grenoble, France.ORCID 0000-0002-1232-8519
Emma L RavenDepartment of Chemistry and Leicester Institute of Structural and Chemical Biology, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester, LE1 7RH, UK. emma.raven@le.ac.uk.
Gordon C K RobertsDepartment of Molecular & Cell Biology and Leicester Institute of Structural and Chemical Biology, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester, LE1 7RH, UK. gcr@le.ac.uk.
University of Leicester · GBInstitut Laue-Langevin · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADPH-cytochrome P450 reductase is a multi-domain redox enzyme which is a key component of the P450 mono-oxygenase drug-metabolizing system. We report studies of the conformational equilibrium of this enzyme using small-angle neutron scattering, under conditions where we are able to control the redox state of the enzyme precisely. Different redox states have a profound effect on domain orientation in the enzyme and we analyse the data in terms of a two-state equilibrium between compact and extended conformations. The effects of ionic strength show that the presence of a greater proportion of the extended form leads to an enhanced ability to transfer electrons to cytochrome c. Domain motion is intrinsically linked to the functionality of the enzyme, and we can define the position of the conformational equilibrium for individual steps in the catalytic cycle.

Indexed as

Electron TransportFibroblastsHumansNADPH-Ferrihemoprotein ReductaseOxidation-ReductionProtein ConformationRecombinant ProteinsScattering, Small AngleNADPH-Ferrihemoprotein ReductaseRecombinant Proteins

Identifiers

PMID28852004
PMCPMC5575293
OpenAlexW2746054425

What OpenQuestion holds

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LicenceCC BY
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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.