Article
Active site of Escherichia coli DNA photolyase: Asn378 is crucial both for stabilizing the neutral flavin radical cofactor and for DNA repair.
Biochemistry - 19 Aug 2008
Xu Lei, Mu Wanmeng, Ding Yanwei, Luo Zhaofeng, Han Qingkai, Bi Fuyong, Wang Yuzhen, Song Qinhua
Abstract excerpt
Escherichia coli DNA photolyase repairs cyclobutane pyrimidine dimer (CPD) in UV-damaged DNA through a photoinduced electron transfer mechanism. The catalytic activity of the enzyme requires fully reduced FAD (FADH (-)). After purification in vitro, the cofactor FADH (-) in photolyase is oxidized into the neutral radical form FADH (*) under aerobic conditions and the enzyme loses its repair function. We have...
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