Evidence map›Paper›PMID 20727847›Full record

ReviewArchives of biochemistry and biophysics2011

Structural control of cytochrome P450-catalyzed ω-hydroxylation.

Jonathan B Johnston, Hugues Ouellet, Larissa M Podust, Paul R Ortiz de Montellano

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Differentiation of Plant and Animal-Derived Cholesterol Using irm-Magnetic resonance in chemistry : MRC · 2026
    Article
  3. Article
  4. Article
  5. Spotlight on CYP4B1.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Expression and Functional Characterization of Breast Cancer-Associated Cytochrome P450 4Z1 inDrug metabolism and disposition: the biological fate of chemicals · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors.

Jonathan B JohnstonDepartment of Pharmaceutical Chemistry, University of California-San Francisco, CA 94158-2517, United States.
Hugues Ouellet
Larissa M Podust
Paul R Ortiz de Montellano

Funding

SELECTIVE DESTRUCTION OF CYTOCHROME P450 BY DRUGSR01GM025515 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2014
$5.6M
Oxygen Sensors and P450 Monooxygenases in Mycobacertium tuberculosisR01AI074824 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 2007 to 2016
$4.3M
SELECTIVE DESTRUCTION OF CYTOCHROME P450 BY DRUGSR37GM025515 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1989 to 1998
–
NIAID NIH HHS AI74824NIAID NIH HHS R01 AI074824NIGMS NIH HHS GM25515NIGMS NIH HHS R01 GM025515NIGMS NIH HHS R37 GM025515
6 · The paper itself

Abstract

The regiospecific or preferential ω-hydroxylation of hydrocarbon chains is thermodynamically disfavored because the ease of C-H bond hydroxylation depends on the bond strength, and the primary C-H bond of a terminal methyl group is stronger than the secondary or tertiary C-H bond adjacent to it. The hydroxylation reaction will therefore occur primarily at the adjacent secondary or tertiary C-H bond unless the protein structure specifically enforces primary C-H bond oxidation. Here we review the classes of enzymes that catalyze ω-hydroxylation and our current understanding of the structural features that promote the ω-hydroxylation of unbranched and methyl-branched hydrocarbon chains. The evidence indicates that steric constraints are used to favor reaction at the ω-site rather than at the more reactive (ω-1)-site.

Indexed as

AnimalsBacteriaBacterial ProteinsCytochrome P-450 Enzyme SystemFatty AcidsHumansHydroxylationModels, MolecularMolecular StructureSubstrate SpecificityBacterial ProteinsCytochrome P-450 Enzyme SystemFatty Acids

Identifiers

PMID20727847
PMCPMC2997901

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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.