Evidence map›Paper›PMID 28872878›Full record

ArticleThe journal of physical chemistry letters2017

Ultrafast Charge-Transfer Dynamics in the Iron-Sulfur Complex of Rhodobacter capsulatus Ferredoxin VI.

Ziliang Mao, Elizabeth C Carroll, Peter W Kim, Stephen P Cramer, Delmar S Larsen

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

Article in The journal of physical chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Understanding Short-Range Electron-Transfer Dynamics in Proteins.The journal of physical chemistry letters · 2019
    Article
  2. 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 2 institutions in 2 countries.

Ziliang MaoDepartment of Chemistry, University of California Davis , One Shields Avenue, Davis, California 95616, United States.
Elizabeth C CarrollDepartment of Chemistry, University of California Davis , One Shields Avenue, Davis, California 95616, United States.
Peter W KimDepartment of Chemistry, University of California Davis , One Shields Avenue, Davis, California 95616, United States.
Stephen P CramerDepartment of Chemistry, University of California Davis , One Shields Avenue, Davis, California 95616, United States.
Delmar S LarsenDepartment of Chemistry, University of California Davis , One Shields Avenue, Davis, California 95616, United States.ORCID http://orcid.org/0000-0003-4522-2689
University of California, Davis · USSandia National Laboratories California · US

Funding

X-Ray Raman and Vibrational Mossbauer of MetalloproteinsR01GM065440 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CRAMER, STEPHEN P. · 2002 to 2025
$7.3M
NIGMS NIH HHS R01 GM065440
6 · The paper itself

Abstract

Iron-sulfur proteins play essential roles in various biological processes. Their electronic structure and vibrational dynamics are key to their rich chemistry but nontrivial to unravel. Here, the first ultrafast transient absorption and impulsive coherent vibrational spectroscopic (ICVS) studies on 2Fe-2S clusters in Rhodobacter capsulatus ferreodoxin VI are characterized. Photoexcitation initiated populations on multiple excited electronic states that evolve into each other in a long-lived charge-transfer state. This suggests a potential light-induced electron-transfer pathway as well as the possibility of using iron-sulfur proteins as photosensitizers for light-dependent enzymes. A tyrosine chain near the active site suggests potential hole-transfer pathways and affirms this electron-transfer pathway. The ICVS data revealed vibrational bands at 417 and 484 cm

Indexed as

Protein ConformationTemperatureElectron Spin Resonance SpectroscopyFerredoxinsGuanineIron-Sulfur ProteinsOxidation-ReductionPhotochemistryRhodobacter capsulatusSpectrum AnalysisSulfurVibrationFerredoxinsGuanineIron-Sulfur ProteinsN(2)-(3-trifluoromethylphenyl)guanineSulfur

Identifiers

PMID28872878
PMCPMC7187928
OpenAlexW2753873716

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.