Premium
The Flavin–Tryptophan Dyad F10T as a Cryptochrome Model Compound: Synthesis and Photochemistry
Author(s) -
Paul Shubhajit,
Meng Lingqiang,
Berger Stefan,
Grampp Günter,
Matysik Jörg,
Wang Xiaojie
Publication year - 2017
Publication title -
chemphotochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.13
H-Index - 18
ISSN - 2367-0932
DOI - 10.1002/cptc.201600025
Subject(s) - cryptochrome , flavin group , photolyase , chemistry , photochemistry , flavin adenine dinucleotide , flavoprotein , tryptophan , electron transfer , photoisomerization , cofactor , biochemistry , catalysis , dna , enzyme , circadian clock , amino acid , isomerization , dna repair , gene
Many animals sense the Earth's magnetic field and use it for navigation. It has been proposed that a light‐dependent quantum effect in cryptochrome photoreceptor proteins residing in the retina allow for such an iron‐free spin‐chemical compass. The primary photochemistry in cryptochromes and photolyases is assumed to be confined mainly in a flavin adenine dinucleotide (FAD) residue and three nearby tryptophan residues. Functional studies require model compounds allowing for direct structural modifications. Inspired by the structure of natural cryptochrome, a flavin–tryptophan dyad (F10T) has been synthesized. 1 H photochemically induced dynamic nuclear polarization (photo‐CIDNP) NMR studies on F10T demonstrate the spin‐correlated radical‐pair formation through photoinduced electron transfer from donor (tryptophan) to acceptor (flavin) moieties under illumination with a white light source similar to sunlight. This is the first model compound of natural cryptochromes with a provision for controlled structural modifications.