Article ID Journal Published Year Pages File Type
1979623 Current Opinion in Structural Biology 2006 9 Pages PDF
Abstract

DNA photolyases are extremely efficient light-driven DNA repair enzymes that use the energy of a blue-light photon to ‘inject’ an electron onto UV-damaged DNA, catalyzing the splitting of mutagenic pyrimidine dimers. By contrast, cryptochromes use blue light to trigger signaling cascades in multicellular organisms, fungi and several prokaryotes. Despite these functional differences, both protein families arose from a common ancestor and share many similarities, such as the overall protein fold, the presence of antenna chromophores and the use of flavin adenine dinucleotide (FAD) as the primary reactive group. Several significant advances in the biophysical and structural characterization of photolyases and cryptochromes are now revealing the details of how light-driven redox reactions can be used for such seemingly different purposes.

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