Evidence map›Paper›PMID 31509280›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

Uno Ferro, a de novo Designed Protein, Binds Transition Metals with High Affinity and Stabilizes Semiquinone Radical Anion.

Jennifer H Yoon, Alona V Kulesha, Zsofia Lengyel-Zhand, Alexander N Volkov, Joel J Rempillo, Areetha D'Souza, Christos Costeas, Cara Chester, Elizabeth R Caselle, Olga V Makhlynets

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  4. Allosteric cooperation in a de novo-designed two-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

10 authors at 2 institutions in 2 countries.

Jennifer H YoonDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Alona V KuleshaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Zsofia Lengyel-ZhandDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Alexander N VolkovVIB Centre for Structural Biology, Vlaams Instituut voor Biotechnologie (VIB), Pleinlaan 2, Brussels, 1050, Belgium.
Joel J RempilloDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Areetha D'SouzaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Christos CosteasDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Cara ChesterDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Elizabeth R CaselleDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Olga V MakhlynetsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.ORCID http://orcid.org/0000-0002-2763-7891
Syracuse University · USVrije Universiteit Brussel · BE

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
A 800 MHz Nuclear Magnetic Resonance Spectrometer in Support of Life Science ReseS10OD012254 · OD · UPSTATE MEDICAL UNIVERSITY · PI WILKENS, STEPHAN · 2013 to 2013
$2.0M
NIGMS NIH HHS P41 GM103521NIH HHS S10 OD012254Syracuse University
6 · The paper itself

Abstract

Metalloenzymes often utilize radicals in order to facilitate chemical reactions. Recently, DeGrado and co-workers have discovered that model proteins can efficiently stabilize semiquinone radical anion produced by oxidation of 3,5-di-tert-butylcatechol (DTBC) in the presence of two zinc ions. Here, we show that the number and the nature of metal ions have relatively minor effect on semiquinone stabilization in model proteins, with a single metal ion being sufficient for radical stabilization. The radical is stabilized by both metal ion, hydrophobic sequestration, and interactions with the hydrophilic residues in the protein interior resulting in a remarkable, nearly 500 mV change in the redox potential of the SQ

Indexed as

Amino Acid SequenceBenzoquinonesBinding SitesCatecholsHydrophobic and Hydrophilic InteractionsIonsKineticsLigandsMetalloproteinsMetalsModels, MolecularOxidation-ReductionProtein BindingProtein ConformationProtein StabilityThermodynamicsBenzoquinonescatecholCatecholsIonsLigandsMetalloproteinsMetalssemiquinone radicalstert-butylcatecholcatechol dioxygenasemetal bindingprotein designprotein NMRsemiquinone radical anion

Identifiers

PMID31509280
PMCPMC6891133
OpenAlexW2973156498

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.