Evidence map›Paper›PMID 29717147›Full record

ArticleScientific reports2018

Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strength.

Krutika Bavishi, Darui Li, Stine Eiersholt, Emma N Hooley, Troels C Petersen, Birger Lindberg Møller, Nikos S Hatzakis, Tomas Laursen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. 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

8 authors at 1 institution in 2 countries.

Krutika BavishiPlant Biochemistry Laboratory, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, 1871, Denmark.
Darui LiDepartment of Chemistry & Nanoscience Center, Thorvaldsensvej 40, University of Copenhagen, Frederiksberg C, 1871, Denmark.
Stine EiersholtDepartment of Chemistry & Nanoscience Center, Thorvaldsensvej 40, University of Copenhagen, Frederiksberg C, 1871, Denmark.
Emma N HooleyThe Nano Spectroscopy Group, Nano Science Center, Department of Chemistry, University of Copenhagen, Copenhagen Ø, 2100, Denmark.
Troels C PetersenNiels Bohr Institute, Blegdamsvej 17, University of Copenhagen, Copenhagen Ø, 2100, Denmark.
Birger Lindberg MøllerPlant Biochemistry Laboratory, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, 1871, Denmark. blm@plen.ku.dk.ORCID 0000-0002-3252-3119
Nikos S HatzakisbioSYNergy, Center for Synthetic Biology, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, 1871, Denmark. hatzakis@nano.ku.dk.ORCID 0000-0003-4202-0328
Tomas LaursenPlant Biochemistry Laboratory, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, 1871, Denmark. tola@plen.ku.dk.
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450 oxidoreductase (POR) is the primary electron donor in eukaryotic cytochrome P450 (CYP) containing systems. A wealth of ensemble biophysical studies of Cytochrome P450 oxidoreductase (POR) has reported a binary model of the conformational equilibrium directing its catalytic efficiency and biomolecular recognition. In this study, full length POR from the crop plant Sorghum bicolor was site-specifically labeled with Cy3 (donor) and Cy5 (acceptor) fluorophores and reconstituted in nanodiscs. Our single molecule fluorescence resonance energy transfer (smFRET) burst analyses of POR allowed the direct observation and quantification of at least three dominant conformational sub-populations, their distribution and occupancies. Moreover, the state occupancies were remodeled significantly by ionic strength and the nature of reconstitution environment, i.e. phospholipid bilayers (nanodiscs) composed of different lipid head group charges vs. detergent micelles. The existence of conformational heterogeneity in POR may mediate selective activation of multiple downstream electron acceptors and association in complexes in the ER membrane.

Indexed as

Osmolar ConcentrationProtein ConformationCarbocyaninesCatalysisCytochrome P-450 Enzyme SystemDetergentsElectronsFluorescence Resonance Energy TransferLipid BilayersMembranesMicellesOxidoreductases Acting on CH-CH Group DonorsPhospholipidsSorghumCarbocyaninescyanine dye 3cyanine dye 5Cytochrome P-450 Enzyme SystemDetergentsLipid BilayersMicellesOxidoreductases Acting on CH-CH Group DonorsPhospholipidsprotochlorophyllide reductase

Identifiers

PMID29717147
PMCPMC5931563
OpenAlexW2801407875

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.