Journal
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 66
Volume 66, Issue -, Pages 691-715Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-physchem-040513-103631
Keywords
nonequilibrium ultrafast dynamics; dimer sequential splitting; electron tunneling pathway; high repair efficiency; flavin functional state; proton-coupled electron transfer
Categories
Funding
- NIGMS NIH HHS [GM074813] Funding Source: Medline
Ask authors/readers for more resources
Photolyase is a flavin photoenzyme that repairs two DNA base damage products induced by ultraviolet (UV) light: cyclobutane pyrimidine dimers and 6-4 photoproducts. With femtosecond spectroscopy and site-directed mutagenesis, investigators have recently made significant advances in our understanding of UV-damaged DNA repair, and the entire enzymatic dynamics can now be mapped out in real time. For dimer repair, six elementary steps have been characterized, including three electron transfer reactions and two bond-breaking processes, and their reaction times have been determined. A unique electron-tunneling pathway was identified, and the critical residues in modulating the repair function at the active site were determined. The dynamic synergy between the elementary reactions for maintaining high repair efficiency was elucidated, and the biological nature of the flavin active state was uncovered. For 6-4 photoproduct repair, a proton-coupled electron transfer repair mechanism has been revealed. The elucidation of electron transfer mechanisms and two repair photocycles is significant and provides a molecular basis for future practical applications, such as in rational drug design for curing skin cancer.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available