Natural and non-natural antenna chromophores in the DNA photolyase from Thermus thermophilus.
X-ray crystallographic and functional analysis of the class I DNA photolyase from Thermus thermophilus revealed the binding of flavin mononucleotide (FMN) as an antenna chromophore. The binding mode of FMN closely coincides with the binding of a deazaflavin-like chromophore in the related class I DNA photolyase from Anacystis nidulans. Compared to the R46E mutant, which lacks a conserved arginine in the binding site for the antenna chromophore, the FMN-comprising holophotolyase exhibits an eightfold higher activity at 450 nm. The facile incorporation of the flavin cofactors 8-hydroxy-deazariboflavin and 8-iodo-8-demethyl-riboflavin into the binding site for the antenna chromophore paves the way for wavelength-tuning of the activity spectra of DNA photolyases by using synthetic flavins.
Klar
Tobias
T
Philipps-Universität Marburg, Fachbereich Chemie, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
Kaiser
Gebhard
G
Hennecke
Ulrich
U
Carell
Thomas
T
Batschauer
Alfred
A
Essen
Lars-Oliver
LO
D001665:Binding Sites; D001688:Biological Products / Q000737:chemistry*; D002384:Catalysis; D018360:Crystallography, X-Ray; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D005415:Flavins / Q000737:chemistry / Q000378:metabolism; D020035:Holoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016963:Thermus thermophilus / Q000201:enzymology*
D001688:Biological Products; D005415:Flavins; D020035:Holoenzymes; D004255:Deoxyribodipyrimidine Photo-Lyase