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Bary W. Wilson, Kris Caputa, Maria A. Stuchly, Jeffrey D. Saffer, Karl C. Davis, Calvin E. Washam, Lloyd G. Washam, Glenn R. Washam and Mark A. Wilson |
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Design and Fabrication of Well Confined Uniform Magnetic Field Exposure Systems |
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Journal Article |
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1994 |
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Bioelectromagnetics |
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15563-577 |
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WP3 Exposure Systems |
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ITIS @ gong @ |
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183 |
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Weber, S.; Biskup, T.; Okafuji, A.; Marino, A.R.; Berthold, T.; Link, G.; Hitomi, K.; Getzoff, E.D.; Schleicher, E.; Norris, J.R.J. |
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Title |
Origin of light-induced spin-correlated radical pairs in cryptochrome |
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Journal Article |
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2010 |
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The Journal of Physical Chemistry. B |
Abbreviated Journal |
J Phys Chem B |
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Volume |
114 |
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45 |
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14745-14754 |
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Keywords |
Animals; Cryptochromes/*chemistry/*metabolism; Electron Spin Resonance Spectroscopy; Electron Transport/radiation effects; Flavin-Adenine Dinucleotide/metabolism; Free Radicals/chemistry/metabolism; *Light; Models, Molecular; Protein Conformation; Xenopus Proteins/chemistry/metabolism; Xenopus laevis |
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Abstract |
Blue-light excitation of cryptochromes and homologues uniformly triggers electron transfer (ET) from the protein surface to the flavin adenine dinucleotide (FAD) cofactor. A cascade of three conserved tryptophan residues has been considered to be critically involved in this photoreaction. If the FAD is initially in its fully oxidized (diamagnetic) redox state, light-induced ET via the tryptophan triad generates a series of short-lived spin-correlated radical pairs comprising an FAD radical and a tryptophan radical. Coupled doublet-pair species of this type have been proposed as the basis, for example, of a biological magnetic compass in migratory birds, and were found critical for some cryptochrome functions in vivo. In this contribution, a cryptochrome-like protein (CRYD) derived from Xenopus laevis has been examined as a representative system. The terminal radical-pair state FAD(*)...W324(*) of X. laevis CRYD has been characterized in detail by time-resolved electron-paramagnetic resonance (TREPR) at X-band microwave frequency (9.68 GHz) and magnetic fields around 345 mT, and at Q-band (34.08 GHz) at around 1215 mT. Different precursor states, singlet versus triplet, of radical-pair formation have been considered in spectral simulations of the experimental electron-spin polarized TREPR signals. Conclusively, we present evidence for a singlet-state precursor of FAD(*)...W324(*) radical-pair generation because at both magnetic fields, where radical pairs were studied by TREPR, net-zero electron-spin polarization has been detected. Neither a spin-polarized triplet precursor nor a triplet at thermal equilibrium can explain such an electron-spin polarization. It turns out that a two-microwave-frequency TREPR approach is essential to draw conclusions on the nature of the precursor electronic states in light-induced spin-correlated radical pair formations. |
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Institute of Physical Chemistry, Albert-Ludwigs-Universitat Freiburg, 79104 Freiburg, Germany. Stefan.Weber@physchem.uni-freiburg.de |
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1520-5207 |
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PMID:20684534 |
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IT'IS @ evaj @ |
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259 |
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Mitsuru Yasui and Yoshihisa Otaka |
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Title |
Facility for Chronic Exposure of Rats to ELF Magnetic Fields |
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Journal Article |
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1993 |
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Bioelectromagnetics |
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14535-544 |
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WP3 Exposure Systems |
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ITIS @ gong @ |
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184 |
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Berndt, A.; Kottke, T.; Breitkreuz, H.; Dvorsky, R.; Hennig, S.; Alexander, M.; Wolf, E. |
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Title |
A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome |
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Journal Article |
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2007 |
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The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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282 |
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17 |
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13011-13021 |
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Animals; Cell Line; *Circadian Rhythm; Cryptochromes; DNA Repair; Deoxyribodipyrimidine Photo-Lyase/chemistry; Drosophila/chemistry/metabolism; Drosophila Proteins/*chemistry/metabolism; Flavin-Adenine Dinucleotide/*chemistry/metabolism; Flavoproteins/*chemistry/metabolism; Oxidation-Reduction; Photochemistry; Photoreceptor Cells, Invertebrate/*chemistry/metabolism |
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Cryptochromes are flavoproteins that are evolutionary related to the DNA photolyases but lack DNA repair activity. Drosophila cryptochrome (dCRY) is a blue light photoreceptor that is involved in the synchronization of the circadian clock with the environmental light-dark cycle. Until now, spectroscopic and structural studies on this and other animal cryptochromes have largely been hampered by difficulties in their recombinant expression. We have therefore established an expression and purification scheme that enables us to purify mg amounts of monomeric dCRY from Sf21 insect cell cultures. Using UV-visible spectroscopy, mass spectrometry, and reversed phase high pressure liquid chromatography, we show that insect cell-purified dCRY contains flavin adenine dinucleotide in its oxidized state (FAD(ox)) and residual amounts of methenyltetrahydrofolate. Upon blue light irradiation, dCRY undergoes a reversible absorption change, which is assigned to the conversion of FAD(ox) to the red anionic FAD(.) radical. Our findings lead us to propose a novel photoreaction mechanism for dCRY, in which FAD(ox) corresponds to the ground state, whereas the FAD(.) radical represents the light-activated state that mediates resetting of the Drosophila circadian clock. |
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Max Planck Institute of Molecular Physiology, Department of Structural Biology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany |
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0021-9258 |
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PMID:17298948 |
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IT'IS @ evaj @ |
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255 |
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Author |
Biskup, T.; Hitomi, K.; Getzoff, E.D.; Krapf, S.; Koslowski, T.; Schleicher, E.; Weber, S. |
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Title |
Unexpected Electron Transfer in Cryptochrome Identified by Time-Resolved EPR Spectroscopy |
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Journal Article |
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2011 |
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Angewandte Chemie International Edition |
Abbreviated Journal |
Angew. Chem. Int. Ed. |
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50 |
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52 |
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12647-12651 |
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1433-7851 |
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IT'IS @ evaj @ |
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245 |
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