Escherichia coli DNA photolyase is a flavoprotein
Journal of Molecular BiologyPublished 1 January 1984
Aziz Sancar, Gwendolyn B. Sancar
Citations122
SJR quartileQ1
SJR score2.21
SNIP1.13
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TL;DR
The purified Escherichia coli DNA photolyase (photoreactivating enzyme) was purified to homogeneity from a strain that greatly overproduces the protein, indicating that FAD is an intrinsic chromophore of the enzyme.
Abstract
Escherichia coli DNA photolyase (photoreactivating enzyme) was purified to homogeneity from a strain that greatly overproduces the protein. The purified enzyme has absorption peaks at 280 and 380 nm, a fluorescence emission peak at 480 nm and, upon denaturation, releases a chromophore that has the spectroscopic properties of flavin adenine dinucleotide (FAD), indicating that FAD is an intrinsic chromophore of the enzyme.
Keywords
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