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Results 1 - 10 of 22 > >>
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) by molecular dynamics simulation and quantum mechanical calculations it is shown that indirect electron tunneling via the protein medium is as important as direct electron transfer from the donor (FADH-) to the acceptor (cyclobutane pyrimidine dimmer). At Met353 site busy electron tunneling traffic is observed. 678738
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) cyclic electron-transfer radical mechanism with two fundamental processes, electron-tunneling pathways and cyclobutane ring splitting, the cyclobutane pyrimidine dimer splits in two sequential steps within 90 ps and the electron tunnels between the cofactor and substrate through a remarkable route with an intervening adenine, dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase, overview 728664
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) dynamics and mechanism of CPD repair by photolyase, detailed overview. In contrast to the computational reaction model the thymine dimer splits by a sequential pathway 748865
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) mechanism 33507, 650226, 652092, 653660
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) mechanism of photoactivation 653629
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction -, 748467
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) on top of the transient formation of tryptophan radicals during photoactivation, evidence is found for oxidation of a tyrosine residue by a tryptophan radical. The tyrosine radical thus formed is reduced by an extrinsic reductant, suggesting that in this case the terminal intrinsic electron donor is tyrosine rather than tryptophan 713768
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview -, 749375
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) radical mechanism through a cyclic redox reaction. Photolyase binds DNA containing a CPD because the thymine dimer distorts the backbone of the DNA. Upon binding to damaged DNA, through ionic interactions between the positively charged groove on the photolyase surface and negatively charged DNA phosphodiester backbone the enzyme pulls the thymine dimer out from within the helix and into the core of the enzyme so that the thymine dimer is within Van der Waals contact with FADH-. It makes a very staple complex, and nothing happens until folate absorbs a photon and transfers the excitation energy to the flavin cofactor. The excited-state flavin, FADH- radical, repairs the thymine dimer by a cyclic redox reaction, and then the enzyme dissociates from the DNA to go on in search of other damage sites to carry out the repair reactions again 746749
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.3cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) reaction mechanism -, 747724
Results 1 - 10 of 22 > >>