Evidence map›Paper›PMID 24443585›Full record

ArticleThe Journal of biological chemistry2014

Structure and biochemical properties of the alkene producing cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 bacterium.

James Belcher, Kirsty J McLean, Sarah Matthews, Laura S Woodward, Karl Fisher, Stephen E J Rigby, David R Nelson, Donna Potts, Michael T Baynham, David A Parker and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
26.5field-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

52 citing papers in PubMed, 192 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Dimer-assisted mechanism of (un)saturated fatty acid decarboxylation for alkene production.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Design of a HProtein science : a publication of the Protein Society · 2022
    Article
  14. Light-driven biocatalytic oxidation.Chemical science · 2022
    Review
  15. Article
  16. Microbial pathways for advanced biofuel production.Biochemical Society transactions · 2022
    Review
  17. Review
  18. Article
  19. Product Distributions of Cytochrome P450 OleTInternational journal of molecular sciences · 2021
    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 3 institutions in 2 countries.

James BelcherManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Kirsty J McLeanManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Sarah MatthewsManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Laura S WoodwardManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Karl FisherManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Stephen E J RigbyManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
David R NelsonDepartment of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.
Donna PottsAgilent Technologies UK Ltd., Lakeside, Cheadle Royal Business Park, Stockport, Cheshire SK8 3GR, United Kingdom.
Michael T BaynhamAgilent Technologies UK Ltd., Lakeside, Cheadle Royal Business Park, Stockport, Cheshire SK8 3GR, United Kingdom.
David A ParkerWesthollow Technology Center, Houston, Texas 77028-3101.
David LeysManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom.
Andrew W MunroManchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, Manchester M1 7DN, United Kingdom. Electronic address: Andrew.Munro@Manchester.ac.uk.
University of Manchester · GBAgilent Technologies (United Kingdom) · GBUniversity of Tennessee Health Science Center · US

Funding

Biotechnology and Biological Sciences Research Council BB/E013007/1Biotechnology and Biological Sciences Research Council BB/F002521/1Biotechnology and Biological Sciences Research Council BB/J012645/1Biotechnology and Biological Sciences Research Council BB/K017802/1
6 · The paper itself

Abstract

The production of hydrocarbons in nature has been documented for only a limited set of organisms, with many of the molecular components underpinning these processes only recently identified. There is an obvious scope for application of these catalysts and engineered variants thereof in the future production of biofuels. Here we present biochemical characterization and crystal structures of a cytochrome P450 fatty acid peroxygenase: the terminal alkene forming OleTJE (CYP152L1) from Jeotgalicoccus sp. 8456. OleTJE is stabilized at high ionic strength, but aggregation and precipitation of OleTJE in low salt buffer can be turned to advantage for purification, because resolubilized OleTJE is fully active and extensively dissociated from lipids. OleTJE binds avidly to a range of long chain fatty acids, and structures of both ligand-free and arachidic acid-bound OleTJE reveal that the P450 active site is preformed for fatty acid binding. OleTJE heme iron has an unusually positive redox potential (-103 mV versus normal hydrogen electrode), which is not significantly affected by substrate binding, despite extensive conversion of the heme iron to a high spin ferric state. Terminal alkenes are produced from a range of saturated fatty acids (C12-C20), and stopped-flow spectroscopy indicates a rapid reaction between peroxide and fatty acid-bound OleTJE (167 s(-1) at 200 μm H2O2). Surprisingly, the active site is highly similar in structure to the related P450BSβ, which catalyzes hydroxylation of fatty acids as opposed to decarboxylation. Our data provide new insights into structural and mechanistic properties of a robust P450 with potential industrial applications.

Indexed as

AlkenesCatalysisCytochrome P-450 Enzyme SystemEnzyme StabilityIndustrial MicrobiologyOsmolar ConcentrationStaphylococcaceaeAlkenesCytochrome P-450 Enzyme SystemBiofuelCrystal StructureCytochrome P450DecarboxylaseElectron Paramagnetic Resonance (EPR)Enzyme KineticsEnzyme MechanismsFatty Acid-binding ProteinHydrogen PeroxideX-ray Crystallography

Identifiers

PMID24443585
PMCPMC3945318
OpenAlexW1963782724

What OpenQuestion holds

Textmetadata
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.