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Time-resolved EPR studies with DNA photolyase: excited-state FADH0 abstracts an electron from Trp-306 to generate FADH-, the catalytically active form of the cofactor.

Photolyase repairs UV-induced cyclobutane-pyrimidine dimers in DNA by photoinduced electron transfer. The enzyme isolated from Escherichia coli contains 5,10-methenyltetrahydrofolate, which functions as the light-harvesting chromophore, and fully reduced flavin adenine dinucleotide (FAD), which func...

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Библиографические подробности
Главные авторы: Kim, S T, Sancar, A, Essenmacher, C, Babcock, G T
Формат: Artigo
Язык:Inglês
Опубликовано: 1993
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC47280/
https://ncbi.nlm.nih.gov/pubmed/8396257
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