Evidence map›Paper›PMID 19293375›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.

Caroline Aldag, Igor A Gromov, Inés García-Rubio, Konstanze von Koenig, Ilme Schlichting, Bernhard Jaun, Donald Hilvert

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. 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
3.0field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  4. Non-Canonical Cytochrome P450 Enzymes in Nature.bioRxiv : the preprint server for biology · 2024
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  5. Review
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  7. The role of basicity in selective C-H bond activation by transition metal-oxidos.Dalton transactions (Cambridge, England : 2003) · 2023
    Review
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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

7 authors at 2 institutions in 2 countries.

Caroline AldagLaboratory of Organic Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
Igor A Gromov
Inés García-Rubio
Konstanze von Koenig
Ilme Schlichting
Bernhard Jaun
Donald Hilvert
ETH Zurich · CHMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unique monooxygenase activity of cytochrome P450cam has been attributed to coordination of a cysteine thiolate to the heme cofactor. To investigate this interaction, we replaced cysteine with the more electron-donating selenocysteine. Good yields of the selenoenzyme were obtained by bacterial expression of an engineered gene containing the requisite UGA codon for selenocysteine and a simplified yet functional selenocysteine insertion sequence (SECIS). The sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2-fold, whereas substrate oxidation becomes partially uncoupled from electron transfer, implying a more complex role for the axial ligand than generally assumed.

Indexed as

Molecular Probe TechniquesProtein EngineeringAmino Acid SubstitutionCamphor 5-MonooxygenaseCloning, MolecularCrystallography, X-RayElectron TransportEscherichia coliHemeKineticsLigandsOxidation-ReductionSelenocysteineCamphor 5-MonooxygenaseHemeLigandsSelenocysteine

Identifiers

PMID19293375
PMCPMC2657087
OpenAlexW2132830102

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.