Evidence map›Paper›PMID 35247855›Full record

ArticleJournal of inorganic biochemistry2022

Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.

Ariel E Schuelke-Sanchez, Amanda R Cornetta, Taylor A J Kocian, Matthew A Conger, Matthew D Liptak

Open access · greenAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. The roles of Asn7 and Trp67 in tuning the ferryl haem form ofDalton transactions (Cambridge, England : 2003) · 2026
    Article
  2. Review
  3. Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025
    Article
  4. Article
  5. 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 at 1 institution in 1 country.

Ariel E Schuelke-SanchezDepartment of Chemistry, University of Vermont, Burlington, VT 05405, United States.
Amanda R CornettaDepartment of Chemistry, University of Vermont, Burlington, VT 05405, United States.
Taylor A J KocianDepartment of Chemistry, University of Vermont, Burlington, VT 05405, United States.
Matthew A CongerDepartment of Chemistry, University of Vermont, Burlington, VT 05405, United States.
Matthew D LiptakDepartment of Chemistry, University of Vermont, Burlington, VT 05405, United States. Electronic address: matthew.liptak@uvm.edu.
University of Vermont · US

Funding

Heme Oxygenases: chemically complex enzymes found in diverse biological pathwaysR35GM139516 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI Matthew D Liptak · 2021 to 2026
$1.7M
Second-Sphere Influences on Oxygen Activation by Non-Canonical Heme OxygenasesR01GM114277 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI LIPTAK, MATTHEW D · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM114277NIGMS NIH HHS R35 GM139516
6 · The paper itself

Abstract

Non-canonical heme oxygenases are enzymes that degrade heme to non-biliverdin products within bacterial heme iron acquisition pathways. These enzymes all contain a conserved second-sphere Trp residue that is essential for enzymatic turnover. Here, UV/Vis absorption (Abs) and circular dichroism (CD) spectroscopies were employed to show that the W67F variant of IsdG perturbs the heme substrate conformation. In general, a dynamic equilibrium between "planar" and "ruffled" substrate conformations exists within non-canonical heme oxygenases, and that the second-sphere Trp favors population of the "ruffled" substrate conformation.

Indexed as

HemeStaphylococcus aureusBacterial ProteinsCatalysisHeme Oxygenase (Decyclizing)IronOxygenasesBacterial ProteinsHemeHeme Oxygenase (Decyclizing)IronOxygenasesBiliverdinEnzyme kineticsHeme oxygenaseMagnetic circular dichroismNuclear magnetic resonanceStaphylobilin

Identifiers

PMID35247855
PMCPMC8930504
OpenAlexW4220806746

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.