DNA photolyases are enzymes that catalyze the light-reaction proceeds most efficiently in polar media, which is in agreement with the observed highly polar flavin binding dependend repair of cis-syn-cyclobutane-thymine dimer UV lesions in a variety of organisms. The basis of the pocket. Investigations with flavin-and deazaflavincontaining model compounds confirmed that the deazaflavin repairreaction is an electron transfer from a reduced and deprotonated flavin cofactor to the dimer unit, which splits functions solely as a photo antenna and allowed to study the dependencies of the antenna function on the protonation spontaneously as its radical anion. A second cofactor, which is either an 8-hydroxy-5-deazaflavin or a methenyl-state of the 8-hydroxy-5-deazaflavin. The ability to mimic the repair reaction with small model compounds allowed finally tetrahydrofolate is required as a photo antenna and ensures efficient light absorption. With the help of model compounds the development of flavin cofactor functionalized oligopeptides. Cofactor peptides with the sequence of the DNA-that are able to mimic all crucial steps of the repair reaction, detailed mechanistic insights into the repair reaction could binding domain of the transcription factor MyoD were shown to be able to repair UV light lesions of DNA within a DNA be obtained. It became clear, that the enzyme requires the reduced flavin in its deprotonated form and that the repair single strand.
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