Evidence map›Paper›PMID 32532989›Full record

ArticleNature communications2020

Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.

April L Lukowski, Jianxin Liu, Jennifer Bridwell-Rabb, Alison R H Narayan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 51 citations in OpenAlex.

  1. Characterization of successiveApplied and environmental microbiology · 2026
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  8. Elucidating the Role of OACS environmental Au · 2024
    Article
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  11. Article
  12. Review
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  14. Article
  15. 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
  16. Engineering Rieske oxygenase activity one piece at a time.Current opinion in chemical biology · 2023
    Review
  17. Article
  18. Article
  19. Definition of a saxitoxin (STX) binding code enables discovery and characterization of the anuran saxiphilin family.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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 at 1 institution in 1 country.

April L Lukowski *Program in Chemical Biology, University of Michigan, Ann Arbor, MI, USA.
Jianxin Liu *Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.ORCID http://orcid.org/0000-0001-5713-434X
Jennifer Bridwell-RabbProgram in Chemical Biology, University of Michigan, Ann Arbor, MI, USA. jebridwe@umich.edu.ORCID http://orcid.org/0000-0002-7437-6217
Alison R H NarayanProgram in Chemical Biology, University of Michigan, Ann Arbor, MI, USA. arhardin@umich.edu.ORCID http://orcid.org/0000-0001-8290-0077
University of Michigan · US

Funding

Undergrad Supplement: Expanding the synthetic utility of natural product biosynthetic enzymesR35GM124880 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alison Narayan · 2017 to 2026
$4.5M
Biocatalytic approaches to antiepileptic drug targetsF31NS111906 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUKOWSKI, APRIL · 2019 to 2020
$49k
NIGMS NIH HHS R35 GM124880NINDS NIH HHS F31 NS111906
6 · The paper itself

Abstract

Biocatalysts that perform C-H hydroxylation exhibit exceptional substrate specificity and site-selectivity, often through the use of high valent oxidants to activate these inert bonds. Rieske oxygenases are examples of enzymes with the ability to perform precise mono- or dioxygenation reactions on a variety of substrates. Understanding the structural features of Rieske oxygenases responsible for control over selectivity is essential to enable the development of this class of enzymes for biocatalytic applications. Decades of research has illuminated the critical features common to Rieske oxygenases, however, structural information for enzymes that functionalize diverse scaffolds is limited. Here, we report the structures of two Rieske monooxygenases involved in the biosynthesis of paralytic shellfish toxins (PSTs), SxtT and GxtA, adding to the short list of structurally characterized Rieske oxygenases. Based on these structures, substrate-bound structures, and mutagenesis experiments, we implicate specific residues in substrate positioning and the divergent reaction selectivity observed in these two enzymes.

Indexed as

Genetic VariationBacterial ProteinsBinding SitesBiocatalysisCatalytic DomainCyanobacteriaHydroxylationIron-Sulfur ProteinsKineticsMixed Function OxygenasesModels, MolecularOxygenasesProtein ConformationProtein MultimerizationSubstrate SpecificityBacterial ProteinsIron-Sulfur ProteinsMixed Function OxygenasesOxygenases

Identifiers

PMID32532989
PMCPMC7293229
OpenAlexW3035559789

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.