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- W1976209043 abstract "The two-electron reduced anionic form of flavin adenine dinucleotide (FADH−) is the catalytically active redox cofactor in DNA photolyase. This enzyme repairs UV-induced cyclobutane pyrimidine dimers (CPD) via a photoinduced electron transfer (PET) reaction, in which the FADH− is excited with blue light. The UV-visible absorption spectra of reduced anionic flavins, characterized decades ago, show a peak at ∼350 nm with a broad shoulder at ∼420 nm. We have shown, through earlier linear dichroism experiments, that these absorption bands arise from two distinct electronic transitions, a controversial result at the time. Here we have used Stark spectroscopy as a complementary approach to substantiate this result. The sensitivity of the amplitude and band shape of the Stark spectra unambiguously resolves the broad absorption band structure into two separate transitions; in fact, an analysis of the Stark data is not possible under the assumption of a single electronic transition. The magnitude of the difference dipole moment of the low energy S0→S1 transition (∼420 nm) is about three times smaller than the S0→S2 transition (∼350 nm). These experimental assignments were supported with TD-DFT calculations which help to assign the direction of charge redistribution. A picture emerges in which the xylene moiety of the isoalloxazine ring becomes electron-rich upon excitation into either absorption band. Interestingly, this part of the isoalloxazine ring is in close proximity to the bound CPD, suggesting that this is the site for PET to the CPD." @default.
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- W1976209043 date "2013-01-01" @default.
- W1976209043 modified "2023-09-26" @default.
- W1976209043 title "Investigation of Excited State Charge Redistribution of the Reduced Anionic Flavin in DNA Photolyase and Simple Solvents by Stark Spectroscopy" @default.
- W1976209043 doi "https://doi.org/10.1016/j.bpj.2012.11.2692" @default.
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