Accueil > Publications > Recherche par années > Années 2000 > 2006

Lukacs, A ; Eker, APM ; Byrdin, M ; Villette, S ; Pan, J ; Brettel, K ; Vos, MH

Role of the middle residue in the triple tryptophan electron transfer chain of DNA photolyase : Ultrafast spectroscopy of a Trp -> Phe mutant

Journal of Physical Chemistry B 110 (32) 15654-15658

publié le

Abstract :

Photoreduction of the semi-reduced flavin adenine dinucleotide cofactor FADH(.) in DNA photolyase from Escherichia coli into FADH(-) involves three tryptophan ( W) residues that form a closely spaced electron-transfer chain FADH(.)-W382-W359-W306. To investigate this process, we have constructed a mutant photolyase in which W359 is replaced by phenylalanine (F). Monitoring its photoproducts by femtosecond spectroscopy, the excited-state FADH(.)* was found to decay in similar to 30 ps, similar as in wild type (WT) photolyase.