Evidence map›Paper›PMID 34009405›Full record

ArticleEuropean biophysics journal : EBJ2021

Structural features and stability of apo- and holo-forms of a simple iron-sulfur protein.

Ana V Almeida, João P Jacinto, João P L Guerra, Bruno J C Vieira, João C Waerenborgh, Nykola C Jones, Søren V Hoffmann, Alice S Pereira, Pedro Tavares

Open access · goldAbstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 58% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

9 authors at 3 institutions in 2 countries.

Ana V AlmeidaMolecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.ORCID http://orcid.org/0000-0002-3235-4183
João P JacintoMolecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.ORCID http://orcid.org/0000-0001-7460-8543
João P L GuerraMolecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.ORCID http://orcid.org/0000-0001-5441-9446
Bruno J C VieiraCentro de Ciências e Tecnologias Nucleares, Instituto Superior Técnico, Universidade de Lisboa, 2695-066, Bobadela LRS, Portugal.ORCID http://orcid.org/0000-0002-6536-9875
João C WaerenborghCentro de Ciências e Tecnologias Nucleares, Instituto Superior Técnico, Universidade de Lisboa, 2695-066, Bobadela LRS, Portugal.ORCID http://orcid.org/0000-0001-6171-4099
Nykola C JonesISA, Department of Physics and Astronomy, Aarhus University, 8000, Aarhus C, Denmark.ORCID http://orcid.org/0000-0002-4081-6405
Søren V HoffmannISA, Department of Physics and Astronomy, Aarhus University, 8000, Aarhus C, Denmark.ORCID http://orcid.org/0000-0002-8018-5433
Alice S PereiraMolecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.ORCID http://orcid.org/0000-0001-5567-6073
Pedro TavaresMolecular Biophysics Laboratory, UCIBIO/Requimte, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal. pedro.tavares@fct.unl.pt.ORCID http://orcid.org/0000-0002-7398-2661
Universidade Nova de Lisboa · PTAarhus University · DKUniversity of Lisbon · PT

Funding

Fundação para a Ciência e a Tecnologia PD/00193/2012Fundação para a Ciência e a Tecnologia PD/BD/135476/2017Fundação para a Ciência e a Tecnologia PD/BD/135477/2017Fundação para a Ciência e a Tecnologia PTDC/BIA-PRO/111485/2009Fundação para a Ciência e a Tecnologia PTDC/QUI/64248/2006Fundação para a Ciência e a Tecnologia SFRH/BD/135056/2017Fundação para a Ciência e a Tecnologia UIDB/00068/2020Fundação para a Ciência e a Tecnologia UIDB/04378/2020Fundação para a Ciência e a Tecnologia UID/Multi/04349/2019
6 · The paper itself

Abstract

Iron-sulfur centers are widespread in living organisms, mostly performing electron transfer functions, either in electron transfer chains or as part of multi-enzymatic complexes, while being also present in enzyme active sites, handling substrate catalysis. Rubredoxin is the simplest iron-sulfur containing protein constituted by a single polypeptide chain of 50 to 60 amino acids, of which four cysteine residues are responsible for metal binding in a tetrahedral coordination sphere. In this manuscript we explore the structure and stability of both apo- and holo-forms of a Rubredoxin from Marinobacter hydrocarbonoclasticus using Synchrotron Radiation Circular Dichroism (SRCD) in combination with other biochemical and spectroscopic techniques. The results are consistent with a holo-protein form containing a monomeric iron center with UV-visible maxima at 760, 578, 494, 386, 356 and 279 nm, an intense EPR resonance with a g value around 4.3 and Mössbauer spectroscopy parameters of δ equal to 0.69 mm/s and ΔE

Indexed as

Circular DichroismElectron Spin Resonance SpectroscopyIronIron-Sulfur ProteinsMarinobacterRubredoxinsSulfurIronIron-Sulfur ProteinsRubredoxinsSulfurIron–sulfur proteinsProtein secondary structureRubredoxinSynchrotron radiation circular dichroism

Identifiers

PMID34009405
OpenAlexW3160836570

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.