Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.99.3 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00914
-
-

Purification (Commentary)

Purification (Comment) Organism
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

Synonyms Comment Organism
DNA photolyase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
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