UV-visible absorption spectrum of FAD and its reduced forms embedded in a cryptochrome protein

• Published in: Physical chemistry chemical physics : PCCP 2020-01, Vol.22 (22), p.12447-12455
• Main Authors: Schwinn, Karno, Ferré, Nicolas, Huix-Rotllant, Miquel
• Format: Article
• Language: English
• Subjects: Absorption spectra; Adenine; Cartesian coordinates; Chemical Sciences; Electromagnetic absorption; Embedding; or physical chemistry; Proteins; Theoretical and; Tryptophan
• ISSN: 1463-9076; 1463-9084
• DOI: 10.1039/d0cp01714k

Cryptochromes are a class of flavoproteins proposed as candidates to explain magnetoreception of animals, plants and bacteria. The main hypothesis is that a biradical is formed upon blue-light absorption by flavin adenine dinucleotide (FAD). In a protein milieu, the oxidized form of FAD can be reduced, leading to four redox derivative forms: anionic and neutral semi-reduced radicals, and anionic and neutral fully reduced forms. All these forms have a characteristic electronic absorption spectrum, with a strong vibrational resolution. Here, we carried out a normal mode analysis at the electrostatic embedding QM/MM level of theory to compute the vibrationally resolved absorption spectra of the five redox forms of FAD embedded in a plant cryptochrome. We show that explicitly accounting for vibrational broadening contributions to electronic transitions is essential to reproduce the experimental spectra. In the case of the neutral radical form of FAD, the absorption spectrum is reproduced only if the presence of a tryptophan radical is considered. Simulation of UV-vis absorption spectra of cryptochromes and flavoproteins requires an explicit account of vibrations of the flavin chromophore embedded in protein.