Evidence map›Paper›PMID 25965587›Full record

ArticleJournal of the American Chemical Society2015

Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2.

Ryan J Martinie, Jovan Livada, Wei-chen Chang, Michael T Green, Carsten Krebs, J Martin Bollinger, Alexey Silakov

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. 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
3.6field-weighted citation impact, top 6% 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, 111 citations in OpenAlex.

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  8. Sequential oxidation of L-lysine by a non-heme iron hydroxylase.bioRxiv : the preprint server for biology · 2025
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  18. Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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 1 institution in 1 country.

Ryan J MartinieDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Jovan LivadaDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Wei-chen ChangDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Michael T GreenDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Carsten KrebsDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
J Martin BollingerDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Alexey SilakovDepartments of †Chemistry and of ‡Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.
Pennsylvania State University · US

Funding

Mechanism of Taurine: Alpha-Ketoglutarate DioxygenaseR01GM069657 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BOLLINGER, JOSEPH M, KREBS, CARSTEN · 2004 to 2016
$2.7M
NIGMS NIH HHS GM-69657NIGMS NIH HHS R01 GM069657
6 · The paper itself

Abstract

The iron(II)- and 2-(oxo)glutarate-dependent (Fe/2OG) oxygenases catalyze an array of challenging transformations, but how individual members of the enzyme family direct different outcomes is poorly understood. The Fe/2OG halogenase, SyrB2, chlorinates C4 of its native substrate, l-threonine appended to the carrier protein, SyrB1, but hydroxylates C5 of l-norvaline and, to a lesser extent, C4 of l-aminobutyric acid when SyrB1 presents these non-native amino acids. To test the hypothesis that positioning of the targeted carbon dictates the outcome, we defined the positions of these three substrates by measuring hyperfine couplings between substrate deuterium atoms and the stable, EPR-active iron-nitrosyl adduct, a surrogate for reaction intermediates. The Fe-(2)H distances and N-Fe-(2)H angles, which vary from 4.2 Å and 85° for threonine to 3.4 Å and 65° for norvaline, rationalize the trends in reactivity. This experimental correlation of position to outcome should aid in judging from structural data on other Fe/2OG enzymes whether they suppress hydroxylation or form hydroxylated intermediates on the pathways to other outcomes.

Indexed as

Bacterial ProteinsMolecular ConformationPseudomonas syringaeSubstrate SpecificityBacterial Proteins

Identifiers

PMID25965587
PMCPMC4456221
OpenAlexW2272601225

What OpenQuestion holds

Textmetadata
LicenceTDM
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.