Literature summary extracted from
Lukacs, A.; Eker, A.P.; Byrdin, M.; Villette, S.; Pan, J.; Brettel, K.; Vos, M.H.
Role of the middle residue in the triple tryptophan electron transfer chain of DNA photolyase: ultrafast spectroscopy of a Trp-->Phe mutant (2006), J. Phys. Chem. B, 110, 15654-15658.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.99.3 |
cloned in Escherichia coli |
Escherichia coli |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.99.3 |
Escherichia coli |
P00914 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.99.3 |
protein is purified by chromatography on heparin-Sepharose CL-6B resin by elution with a 0.1-1.1 M NaCl gradient in 0.01 M potassium phosphate pH 7.0, 10 mM 2-mercaptoethanol, followed by chromatography on SP-Sepharose Fast Flow resin eluted with a 0.04-0.3 M NaCl gradient. To minimize oxidation of the FAD chromophore during purification, solutions are flushed with and kept under nitrogen |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.99.3 |
DNA photolyase |
- |
Escherichia coli |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.1.99.3 |
FADH2 |
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step. |
Escherichia coli |
|