Evidence map›Paper›PMID 24289221›Full record

ArticleBiochemistry2013

Femtosecond dynamics of short-range protein electron transfer in flavodoxin.

Ting-Fang He, Lijun Guo, Xunmin Guo, Chih-Wei Chang, Lijuan Wang, Dongping Zhong

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Understanding Short-Range Electron-Transfer Dynamics in Proteins.The journal of physical chemistry letters · 2019
    Article
  14. Article
  15. Circadian clock activity of cryptochrome relies on tryptophan-mediated photoreduction.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Review
  18. Dynamics and mechanisms of DNA repair by photolyase.Physical chemistry chemical physics : PCCP · 2015
    Review
  19. 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

6 authors at 1 institution in 1 country.

Ting-Fang HeDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
Lijun Guo
Xunmin Guo
Chih-Wei Chang
Lijuan Wang
Dongping Zhong
The Ohio State University · US

Funding

Functional Dynamics and Molecular Mechanism of PhotolayseR01GM074813 · NIGMS · OHIO STATE UNIVERSITY · PI ZHONG, DONGPING · 2007 to 2016
$2.6M
NIGMS NIH HHS GM074813,NIGMS NIH HHS R01 GM074813
6 · The paper itself

Abstract

Intraprotein electron transfer (ET) in flavoproteins is important for understanding the correlation of their redox, configuration, and reactivity at the active site. Here, we used oxidized flavodoxin as a model system and report our complete characterization of a photoinduced redox cycle from the initial charge separation in 135-340 fs to subsequent charge recombination in 0.95-1.6 ps and to the final cooling relaxation of the product(s) in 2.5-4.3 ps. With 11 mutations at the active site, we observed that these ultrafast ET dynamics, much faster than active-site relaxation, mainly depend on the reduction potentials of the electron donors with minor changes caused by mutations, reflecting a highly localized ET reaction between the stacked donor and acceptor at a van der Waals distance and leading to a gas-phase type of bimolecular ET reaction confined in the active-site nanospace. Significantly, these ultrafast ET reactions ensure our direct observation of vibrationally excited reaction product(s), suggesting that the back ET barrier is effectively reduced because of the decrease in the total free energy in the Marcus inverted region, leading to the accelerated charge recombination. Such vibrationally coupled charge recombination should be a general feature of flavoproteins with similar configurations and interactions between the cofactor flavin and neighboring aromatic residues.

Indexed as

ElectronsModels, MolecularAmino Acid SubstitutionBacterial ProteinsBinding SitesDesulfovibrio vulgarisFlavin MononucleotideFlavodoxinKineticsLightMutagenesis, Site-DirectedMutant ProteinsOxidation-ReductionPhotochemical ProcessesTryptophanTyrosineBacterial ProteinsFlavin MononucleotideFlavodoxinMutant ProteinsTryptophanTyrosine

Identifiers

PMID24289221
PMCPMC3909472
OpenAlexW2062059832

What OpenQuestion holds

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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.