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- W2011874527 abstract "DNA photolyase recognizes ultraviolet-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer by a light-activated electron transfer reaction between the flavin adenine dinucleotide, the electron donor, and cyclobutane pyrimidine dimer, the electron acceptor. Theoretical analysis of the electron-tunneling pathways of the DNA photolyase derived from Anacystis nidulans can reveal the active role of the protein environment in the electron transfer reaction. Here, we report the unexpectedly important role of the single methionine residue, Met-353, where busy trafficking of electron-tunneling currents is observed. The amino acid conservation pattern of Met-353 in the homologous sequences perfectly correlates with experimentally verified annotation as photolyases. The bioinformatics sequence analysis also suggests that the residue plays a pivotal role in biological function. Consistent findings from different disciplines of computational biology strongly suggest the pivotal role of Met-353 in the biological function of DNA photolyase." @default.
- W2011874527 created "2016-06-24" @default.
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- W2011874527 creator A5075030102 @default.
- W2011874527 date "2008-03-01" @default.
- W2011874527 modified "2023-10-16" @default.
- W2011874527 title "Discrimination of Class I Cyclobutane Pyrimidine Dimer Photolyase from Blue Light Photoreceptors by Single Methionine Residue" @default.
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- W2011874527 doi "https://doi.org/10.1529/biophysj.107.119248" @default.
- W2011874527 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2257881" @default.
- W2011874527 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18055535" @default.
- W2011874527 hasPublicationYear "2008" @default.
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