Structural basis of the radical pair state in photolyases and cryptochromes.
Journal
Chemical communications (Cambridge, England)
ISSN: 1364-548X
Titre abrégé: Chem Commun (Camb)
Pays: England
ID NLM: 9610838
Informations de publication
Date de publication:
14 Apr 2022
14 Apr 2022
Historique:
pubmed:
31
3
2022
medline:
16
4
2022
entrez:
30
3
2022
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 35352724
doi: 10.1039/d2cc00376g
pmc: PMC9008703
doi:
Substances chimiques
Amino Acids
0
Cryptochromes
0
Flavin-Adenine Dinucleotide
146-14-5
Tryptophan
8DUH1N11BX
Deoxyribodipyrimidine Photo-Lyase
EC 4.1.99.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4889-4892Références
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