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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.

The reaction of allyltrimethylsilane with a-keto esters in the presence of titanium tetrachloride afforded a y8-unsaturated a-hydroxyvalerate in high yield, which with chiral a-keto esters in asymmetric synthesis gave 1 6 4 5 % enantiomeric excess product.RECENTLY, allyltrimethylsilane was shown to be potentially useful in the allylation of acyl halides' or carbonyl compounds.2 We found that the reaction of allyltrimethylsilane with a-keto esters in the presence of titanium tetrachloride proceeded readily even a t -78 "C to give @unsaturated a-hydroxyvalerates in high yields [equation 6f-I(1) ; Table 13. Although alkylation or arylation of a-keto esters using Grignard reagents is well known,3 the allylation of a-keto esters gave only poor yields.Thus, the present reaction may provide a useful route to $-unsaturated a-hydroxyvalerates.

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