ArticleThe journal of physical chemistry. B2024
Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein.
Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026Article
- The energy landscape of N-ribosidic bond cleavage catalysed by 2'-deoxynucleoside 5'-phosphate N-hydrolase 1.The Biochemical journal · 2025Article
- Cryptochrome 4b protein is probably irrelevant for radical pair-based magnetoreception in the European robin.Journal of the Royal Society, Interface · 2025Article
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5 authors.
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Abstract
It is still a puzzle that has not been entirely solved how migratory birds utilize the Earth's magnetic field for biannual migration. The most consistent explanation thus far is rooted in the modulation of the biological function of the cryptochrome 4 (Cry4) protein by an external magnetic field. This phenomenon is closely linked with the flavin adenine dinucleotide (FAD) cofactor that is noncovalently bound in the protein. Cry4 is activated by blue light, which is absorbed by the FAD cofactor. Subsequent electron and proton transfers trigger radical pair formation in the protein, which is sensitive to the external magnetic field. An important long-lasting redox state of the FAD cofactor is the signaling (FADH
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