Evidence map›Paper›PMID 36997762›Full record

ArticleNature structural & molecular biology2023

Structural basis for enzymatic terminal C-H bond functionalization of alkanes.

Jin Chai, Gongrui Guo, Sean M McSweeney, John Shanklin, Qun Liu

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  6. Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Journal of the American Chemical Society · 2025
    Article
  16. Generalization of Classification of AlkB Family Alkane Monooxygenases fromInternational journal of molecular sciences · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023
    Review
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 at 1 institution in 1 country.

Jin Chai *Biology Department, Brookhaven National Laboratory, Upton, NY, USA.ORCID 0000-0002-4760-5811
Gongrui Guo *Biology Department, Brookhaven National Laboratory, Upton, NY, USA.ORCID 0000-0001-8985-5870
Sean M McSweeneyNSLS-II, Brookhaven National Laboratory, Upton, NY, USA.
John ShanklinBiology Department, Brookhaven National Laboratory, Upton, NY, USA. shanklin@bnl.gov.ORCID 0000-0002-6774-8043
Qun LiuBiology Department, Brookhaven National Laboratory, Upton, NY, USA. qunliu@bnl.gov.ORCID 0000-0002-1179-290X
Brookhaven National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alkane monooxygenase (AlkB) is a widely occurring integral membrane metalloenzyme that catalyzes the initial step in the functionalization of recalcitrant alkanes with high terminal selectivity. AlkB enables diverse microorganisms to use alkanes as their sole carbon and energy source. Here we present the 48.6-kDa cryo-electron microscopy structure of a natural fusion from Fontimonas thermophila between AlkB and its electron donor AlkG at 2.76 Å resolution. The AlkB portion contains six transmembrane helices with an alkane entry tunnel within its transmembrane domain. A dodecane substrate is oriented by hydrophobic tunnel-lining residues to present a terminal C-H bond toward a diiron active site. AlkG, an [Fe-4S] rubredoxin, docks via electrostatic interactions and sequentially transfers electrons to the diiron center. The archetypal structural complex presented reveals the basis for terminal C-H selectivity and functionalization within this broadly distributed evolutionary class of enzymes.

Indexed as

AlkanesCryoelectron MicroscopyCytochrome P-450 CYP4AAlkanesCytochrome P-450 CYP4A

Identifiers

PMID36997762
PMCPMC10113152
OpenAlexW4362460102

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.