Evidence map›Paper›PMID 29858244›Full record

ArticleThe Journal of biological chemistry2018

Noncovalent interactions dominate dynamic heme distortion in cytochrome P450 4B1.

Gareth K Jennings, Mei-Hui Hsu, Lisa S Shock, Eric F Johnson, John C Hackett

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Spotlight on CYP4B1.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. 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

5 authors.

Gareth K JenningsMassey Cancer Center and Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298.
Mei-Hui HsuDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, California 92037.
Lisa S ShockMassey Cancer Center and Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298.
Eric F JohnsonDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, California 92037. Electronic address: johnson@scripps.edu.
John C HackettMassey Cancer Center and Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298. Electronic address: john.hackett@vcuhealth.org.

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
CYTOCHROME P450 POLYMORPHISMR01GM031001 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI JOHNSON, ERIC F · 1985 to 2022
$16.2M
Computational and Vibrational Probes of CYP3A4 Solution DynamicsR01GM114168 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI HACKETT, JOHN C · 2015 to 2018
$1.3M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM031001NIGMS NIH HHS R01 GM114168
6 · The paper itself

Abstract

Cytochrome P450 4B1 (4B1) functions in both xenobiotic and endobiotic metabolism. An ester linkage between Glu-310 in 4B1 and the 5-methyl group of heme facilitates preferential hydroxylation of terminal (ω) methyl groups of hydrocarbons (HCs) and fatty acids compared with ω-1 sites bearing weaker C-H bonds. This preference is retained albeit diminished 4-fold for the E310A mutant, but the reason for this is unclear. Here, a crystal structure of the E310A-octane complex disclosed that noncovalent interactions maintain heme deformation in the absence of the ester linkage. Consistent with the lower symmetry of the heme, resonance Raman (RR) spectroscopy revealed large enhancements of RR peaks for high-spin HC complexes of 4B1 and the E310A mutant relative to P450 3A4. Whereas these enhancements were diminished in RR spectra of a low-spin 4B1-

Indexed as

AnimalsAryl Hydrocarbon HydroxylasesCatalytic DomainCrystallography, X-RayHemeHydroxylationModels, MolecularOxidation-ReductionRabbitsSpectrum Analysis, RamanStereoisomerismSubstrate SpecificityAryl Hydrocarbon Hydroxylasescytochrome P-450 CYP4B1HemeCYP4B1cytochrome P450hemeheme distortionhydrocarbonomega-hydroxylationRaman spectroscopyregiochemistryregioselectivityresonance ramansubstrate specificityultraviolet-visible spectroscopyX-ray crystallography

Identifiers

PMID29858244
PMCPMC6065186

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.