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Proc Natl Acad Sci U S A
2002 Feb 05;993:1319-22. doi: 10.1073/pnas.032469399.
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Photoactivation of the flavin cofactor in Xenopus laevis (6 - 4) photolyase: observation of a transient tyrosyl radical by time-resolved electron paramagnetic resonance.
Weber S
,
Kay CW
,
Mögling H
,
Möbius K
,
Hitomi K
,
Todo T
.
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The light-induced electron transfer reaction of flavin cofactor photoactivation in Xenopus laevis (6-4) photolyase has been studied by continuous-wave and time-resolved electron paramagnetic resonance spectroscopy. When the photoactivation is initiated from the fully oxidized form of the flavin, a neutral flavin radical is observed as a long-lived paramagnetic intermediate of two consecutive single-electron reductions under participation of redox-active amino acid residues. By time-resolved electron paramagnetic resonance, a spin-polarized transient radical-pair signal was detected that shows remarkable differences to the signals observed in the related cyclobutane pyrimidine dimer photolyase enzyme. In (6-4) photolyase, a neutral tyrosine radical has been identified as the final electron donor, on the basis of the characteristic line width, hyperfine splitting pattern, and resonance magnetic field position of the tyrosine resonances of the transient radical pair.
Aubert,
Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans.
1999, Pubmed
Aubert,
Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans.
1999,
Pubmed
Aubert,
Intraprotein radical transfer during photoactivation of DNA photolyase.
2000,
Pubmed
Bleifuss,
Tryptophan and tyrosine radicals in ribonucleotide reductase: a comparative high-field EPR study at 94 GHz.
2001,
Pubmed
Carell,
The mechanism of action of DNA photolyases.
2001,
Pubmed
Cashmore,
Cryptochromes: blue light receptors for plants and animals.
1999,
Pubmed
Cheung,
Pathways of electron transfer in Escherichia coli DNA photolyase: Trp306 to FADH.
1999,
Pubmed
Deisenhofer,
DNA photolyases and cryptochromes.
2000,
Pubmed
Gindt,
Origin of the transient electron paramagnetic resonance signals in DNA photolyase.
1999,
Pubmed
Heelis,
Photochemical properties of Escherichia coli DNA photolyase: a flash photolysis study.
1986,
Pubmed
Heelis,
Excited-state properties of Escherichia coli DNA photolyase in the picosecond to millisecond time scale.
1990,
Pubmed
Himo,
Density functional calculations on model tyrosyl radicals.
1997,
Pubmed
Hitomi,
Binding and catalytic properties of Xenopus (6-4) photolyase.
1997,
Pubmed
,
Xenbase
Jorns,
Identification of a neutral flavin radical and characterization of a second chromophore in Escherichia coli DNA photolyase.
1984,
Pubmed
Kanai,
Molecular evolution of the photolyase-blue-light photoreceptor family.
1997,
Pubmed
Kay,
EPR, ENDOR, and TRIPLE resonance spectroscopy on the neutral flavin radical in Escherichia coli DNA photolyase.
1999,
Pubmed
Kiener,
Purification and properties of Methanobacterium thermoautotrophicum DNA photolyase.
1989,
Pubmed
Kim,
Time-resolved EPR studies with DNA photolyase: excited-state FADH0 abstracts an electron from Trp-306 to generate FADH-, the catalytically active form of the cofactor.
1993,
Pubmed
Li,
Active site of DNA photolyase: tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro.
1991,
Pubmed
Massey,
On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones.
1966,
Pubmed
Müller,
The flavin redox-system and its biological function.
1983,
Pubmed
Nakajima,
Cloning and characterization of a gene (UVR3) required for photorepair of 6-4 photoproducts in Arabidopsis thaliana.
1998,
Pubmed
,
Xenbase
Park,
Crystal structure of DNA photolyase from Escherichia coli.
1995,
Pubmed
Payne,
The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro.
1987,
Pubmed
Rustandi,
Photoinduced spin-polarized radical pair formation in a DNA photolyase.substrate complex at low temperature.
1995,
Pubmed
Sancar,
Enzymatic photoreactivation: 50 years and counting.
2000,
Pubmed
Sancar,
Escherichia coli DNA photolyase is a flavoprotein.
1984,
Pubmed
Sancar,
Action mechanism of Escherichia coli DNA photolyase. III. Photolysis of the enzyme-substrate complex and the absolute action spectrum.
1987,
Pubmed
Sancar,
Structure and function of DNA photolyase.
1994,
Pubmed
Todo,
A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4)photoproducts.
1993,
Pubmed
Todo,
Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family.
1996,
Pubmed
Todo,
Flavin adenine dinucleotide as a chromophore of the Xenopus (6-4)photolyase.
1997,
Pubmed
,
Xenbase
Todo,
Functional diversity of the DNA photolyase/blue light receptor family.
1999,
Pubmed
Un,
245 GHz high-field EPR study of tyrosine-D zero and tyrosine-Z zero in mutants of photosystem II.
1996,
Pubmed
Zhao,
Reaction mechanism of (6-4) photolyase.
1997,
Pubmed
Zhao,
(6-4) photolyase: light-dependent repair of DNA damage.
1998,
Pubmed