Evidence map›Paper›PMID 18227133›Full record

ArticleBiophysical journal2008

Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome C.

Katia C U Mugnol, Rômulo A Ando, Rafael Y Nagayasu, Adelaide Faljoni-Alario, Sergio Brochsztain, Paulo S Santos, Otaciro R Nascimento, Iseli L Nantes

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
6.7field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Selectivity and Reactivity of ZrFrontiers in chemistry · 2018
    Article
  7. Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Journal of the American Chemical Society · 2016
    Article
  8. Article
  9. Article
  10. Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  11. Article
  12. Article
  13. Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010
    Article
  14. Structural and thermodynamic behavior of cytochrome c assembled with glutathione-covered gold nanoparticles.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009
    Article
  15. 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

8 authors at 3 institutions in 1 country.

Katia C U MugnolCentro Interdisciplinar de Investigação Bioquímica, Prédio I, Universidade de Mogi das Cruzes, CP 411, Mogi das Cruzes, SP, CEP 08780-911, Brazil.
Rômulo A Ando
Rafael Y Nagayasu
Adelaide Faljoni-Alario
Sergio Brochsztain
Paulo S Santos
Otaciro R Nascimento
Iseli L Nantes
Universidade de Mogi das Cruzes · BRUniversidade de São Paulo · BRUniversidade Federal de São Carlos · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The alternative low-spin states of Fe(3+) and Fe(2+) cytochrome c induced by SDS or AOT/hexane reverse micelles exhibited the heme group in a less rhombic symmetry and were characterized by electron paramagnetic resonance, UV-visible, CD, magnetic CD, fluorescence, and Raman resonance. Consistent with the replacement of Met(80) by another strong field ligand at the sixth heme iron coordination position, Fe(3+) ALSScytc exhibited 1-nm Soret band blue shift and epsilon enhancement accompanied by disappearance of the 695-nm charge transfer band. The Raman resonance, CD, and magnetic CD spectra of Fe(3+) and Fe(2+) ALSScytc exhibited significant changes suggestive of alterations in the heme iron microenvironment and conformation and should not be assigned to unfold because the Trp(59) fluorescence remained quenched by the neighboring heme group. ALSScytc was obtained with His(33) and His(26) carboxyethoxylated horse cytochrome c and with tuna cytochrome c (His(33) replaced by Asn) pointing out Lys(79) as the probable heme iron ligand. Fe(3+) ALSScytc retained the capacity to cleave tert-butylhydroperoxide and to be reduced by dithiothreitol and diphenylacetaldehyde but not by ascorbate. Compatible with a more open heme crevice, ALSScytc exhibited a redox potential approximately 200 mV lower than the wild-type protein (+220 mV) and was more susceptible to the attack of free radicals.

Indexed as

Models, ChemicalAnimalsComputer SimulationCytochromes cHorsesIronModels, MolecularMyocardiumProtein ConformationSpectrum AnalysisSpin LabelsCytochromes cIronSpin Labels

Identifiers

PMID18227133
PMCPMC2367172
OpenAlexW2057527679

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.