The mechanism by which cryptochrome (CRY) proteins are capable of sensing weak magnetic fields (e.g., the geomagnetic field: ~50 μT) was suggested to be mediated by spin-correlated radical pairs (SCRPs) comprising a flavin adenine dinucleotide (FAD) radical and a tryptophan (Trp) radical which are formed simultaneously by light-induced electron transfer (ET). Here, the authors use time-resolved electron paramagnetic resonance (TREPR) spectroscopy to provide evidence for direct photoinduced ET responsible for the formation of long-lived SCRPs comprising a flavin (Fl) radical and a guanine (G) radical in flavin-tethered single- and double-stranded DNA oligomers.
- Yoshimi Oka
- Florian Quintes
- Katsuya Inoue
