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- W563878929 abstract "We studied the light-induced reactions of the (6-4) photolyase, a flavoenzyme of the cryptochrome/photolyase family that repairs the UV-induced (6-4) photodamage in DNA with the aid of blue light. We studied this photorepair reaction as well as the light-induced cofactor reduction called photoactivation that the enzyme uses to bring itself to a repair-active state in the (6-4) photolyase from Xenopus laevis. We have studied the photoactivation of the FADox cofactor of the enzyme using femtosecond polarised transient absorption spectroscopy. We observed a sub-picosecond electron transfer (~400 fs) after excitation of the FADox cofactor. We were able to characterise a tryptophan residue as the electron donor. We sought to differentiate the spectroscopically identical but differently oriented tryptophan residues within the protein’s photoactivation site by transient anisotropy measurements. Our results suggest that the photoactivation mechanism is not fully compatible with the mechanism thought to be conserved among photolyases: an electron transfer mechanism via electron hopping along a chain of three highly conserved tryptophan residues.Using series of single turnover flashes, we have found that the repair reaction proceeds by a successive two-photon mechanism. The first photon converts the (6-4) lesion into a metastable intermediate X, the lifetime of which is ~2 min. Absorption of a second photon within the lifetime of X results to the restoration of intact nucleobases. In light of our findings, the reaction was also studied by femtosecond transient absorption spectroscopy." @default.
- W563878929 created "2016-06-24" @default.
- W563878929 creator A5082198919 @default.
- W563878929 date "2014-12-15" @default.
- W563878929 modified "2023-09-23" @default.
- W563878929 title "Studies on the Primary Mechanisms of (6-4) photolyase : Photoactivation and DNA Repair" @default.
- W563878929 hasPublicationYear "2014" @default.
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