dc.contributor.author | Prytkova, T. R. | en |
dc.contributor.author | Beratan, David N. | en |
dc.contributor.author | Skourtis, Spiros S. | en |
dc.creator | Prytkova, T. R. | en |
dc.creator | Beratan, David N. | en |
dc.creator | Skourtis, Spiros S. | en |
dc.date.accessioned | 2019-12-02T15:32:29Z | |
dc.date.available | 2019-12-02T15:32:29Z | |
dc.date.issued | 2007 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/59015 | |
dc.description.abstract | Cyclobutane dimer photolyases are proteins that bind to UV-damaged DNA containing cyclobutane pyrimidine dimer lesions. They repair these lesions by photo-induced electron transfer. The electron donor cofactor of a photolyase is a two-electron-reduced flavin adenine dinucleotide (FADH-). When FADH- is photo-excited, it transfers an electron from an excited π → π* singlet state to the pyrimidine dimer lesion of DNA. We compute the lowest excited singlet states of FADH- using ab initio (time-dependent density functional theory and time-dependent Hartree-Fock), and semiempirical (INDO/S configuration interaction) methods. The calculations show that the two lowest π → π* singlet states of FADH- are localized on the side of the flavin ring that is proximal to the dimer lesion of DNA. For the lowest-energy donor excited state of FADH-, we compute the conformationally averaged electronic coupling to acceptor states of the thymine dimer. The coupling calculations are performed at the INDO/S level, on donor-acceptor cofactor conformations obtained from molecular dynamics simulations of the solvated protein with a thymine dimer docked in its active site. These calculations demonstrate that the localization of the 1FADH-* donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer. © 2007 by The National Academy of Sciences of the USA. | en |
dc.source | Proceedings of the National Academy of Sciences of the United States of America | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-33846546681&doi=10.1073%2fpnas.0605319104&partnerID=40&md5=915b58825eb4f9d1e5ee273773f305be | |
dc.subject | Computer Simulation | en |
dc.subject | article | en |
dc.subject | priority journal | en |
dc.subject | thymine | en |
dc.subject | DNA | en |
dc.subject | Escherichia coli | en |
dc.subject | density functional theory | en |
dc.subject | Electrons | en |
dc.subject | ultraviolet radiation | en |
dc.subject | electron transport | en |
dc.subject | conformation | en |
dc.subject | molecular dynamics | en |
dc.subject | DNA damage | en |
dc.subject | Protein Structure, Tertiary | en |
dc.subject | protein DNA binding | en |
dc.subject | enzyme active site | en |
dc.subject | Models, Molecular | en |
dc.subject | solvation | en |
dc.subject | Photochemistry | en |
dc.subject | cyclobutane | en |
dc.subject | Deoxyribodipyrimidine Photo-Lyase | en |
dc.subject | deoxyribodipyrimidine photolyase | en |
dc.subject | Dimerization | en |
dc.subject | flavine adenine nucleotide | en |
dc.subject | pyrimidine dimer | en |
dc.title | Photoselected electron transfer pathways in DNA photolyase | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1073/pnas.0605319104 | |
dc.description.volume | 104 | |
dc.description.issue | 3 | |
dc.description.startingpage | 802 | |
dc.description.endingpage | 807 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Φυσικής / Department of Physics | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :51</p> | en |
dc.source.abbreviation | Proc.Natl.Acad.Sci.U.S.A. | en |
dc.contributor.orcid | Skourtis, Spiros S. [0000-0002-5834-248X] | |
dc.gnosis.orcid | 0000-0002-5834-248X | |