Evidence map›Paper›PMID 23430261›Full record

ArticleThe Journal of biological chemistry2013

Variable electron transfer pathways in an amphibian cryptochrome: tryptophan versus tyrosine-based radical pairs.

Till Biskup, Bernd Paulus, Asako Okafuji, Kenichi Hitomi, Elizabeth D Getzoff, Stefan Weber, Erik Schleicher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
12.5field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. FeSBCP analogue from cyanobacteria: insights from in vitro and in silico studies.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  3. Article
  4. Article
  5. Elucidation of a distinct photoreduction pathway in class IIProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
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  14. Article
  15. Article
  16. 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
  17. Article
  18. Article
  19. Article
  20. Magnetic Fields Modulate Blue-Light-Dependent Regulation of Neuronal Firing by Cryptochrome.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    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

7 authors at 3 institutions in 4 countries.

Till BiskupDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, United Kingdom.
Bernd Paulus
Asako Okafuji
Kenichi Hitomi
Elizabeth D Getzoff
Stefan Weber
Erik Schleicher
University of Freiburg · DEScripps Research Institute · USUniversity of Oxford · GB

Funding

STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
NIGMS NIH HHS GM37684NIGMS NIH HHS R01 GM037684
6 · The paper itself

Abstract

Electron transfer reactions play vital roles in many biological processes. Very often the transfer of charge(s) proceeds stepwise over large distances involving several amino acid residues. By using time-resolved electron paramagnetic resonance and optical spectroscopy, we have studied the mechanism of light-induced reduction of the FAD cofactor of cryptochrome/photolyase family proteins. In this study, we demonstrate that electron abstraction from a nearby amino acid by the excited FAD triggers further electron transfer steps even if the conserved chain of three tryptophans, known to be an effective electron transfer pathway in these proteins, is blocked. Furthermore, we were able to characterize this secondary electron transfer pathway and identify the amino acid partner of the resulting flavin-amino acid radical pair as a tyrosine located at the protein surface. This alternative electron transfer pathway could explain why interrupting the conserved tryptophan triad does not necessarily alter photoreactions of cryptochromes in vivo. Taken together, our results demonstrate that light-induced electron transfer is a robust property of cryptochromes and more intricate than commonly anticipated.

Indexed as

AmphibiansAnimalsCryptochromesDeoxyribodipyrimidine Photo-LyaseElectron Spin Resonance SpectroscopyElectron TransportFlavin-Adenine DinucleotideKineticsLightModels, MolecularMolecular ConformationOptics and PhotonicsPhotochemistrySpectrophotometry, UltravioletTryptophanTyrosineCryptochromesDeoxyribodipyrimidine Photo-LyaseFlavin-Adenine DinucleotideTryptophanTyrosine

Identifiers

PMID23430261
PMCPMC3610996
OpenAlexW1967301999

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.