ArticleChemical communications (Cambridge, England)2022
Structural basis of the radical pair state in photolyases and cryptochromes.
Article in Chemical communications (Cambridge, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Weak Radiofrequency Field Effects on Biological Systems Mediated through the Radical Pair Mechanism.Chemical reviews · 2025Review
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.Nature chemistry · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- 'Seeing' the electromagnetic spectrum: spotlight on the cryptochrome photocycle.Frontiers in plant science · 2024Review
- A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.Nature communications · 2023Article
- Effects of weak static magnetic fields on the development of seedlings of Arabidopsis thaliana.Protoplasma · 2023Article
- Insights into Molecular Structure of Pterins Suitable for Biomedical Applications.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptophan radical rearrange, opening it up to the solvent. The structure explains how the protein environment stabilizes the radical pair state, which is crucial for function of (6-4) photolyases and cryptochromes.
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