Structural basis of the radical pair state in photolyases and cryptochromes
| Autor: | Andrea Cellini, Madan Kumar Shankar, Weixiao Yuan Wahlgren, Amke Nimmrich, Antonia Furrer, Daniel James, Maximilian Wranik, Sylvain Aumonier, Emma V. Beale, Florian Dworkowski, Jörg Standfuss, Tobias Weinert, Sebastian Westenhoff |
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| Rok vydání: | 2022 |
| Předmět: |
Metals and Alloys
Biochemistry and Molecular Biology Tryptophan General Chemistry Catalysis Surfaces Coatings and Films Electronic Optical and Magnetic Materials Cryptochromes Materials Chemistry Ceramics and Composites Flavin-Adenine Dinucleotide Animals Amino Acids Deoxyribodipyrimidine Photo-Lyase Biokemi och molekylärbiologi |
| Zdroj: | Chemical communications (Cambridge, England). 58(31) |
| ISSN: | 1364-548X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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