Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy

Kottke T, Batschauer A, Ahmad M, Heberle J (2006)
Biochemistry 45(8): 2472-2479.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Kottke, TilmanUniBi ; Batschauer, Alfred; Ahmad, Margaret; Heberle, Joachim
Einrichtung
Fakultät für Chemie > Physikalische und Biophysikalische Chemie
Erscheinungsjahr
2006
Zeitschriftentitel
Biochemistry
Band
45
Ausgabe
8
Seite(n)
2472-2479
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1600212

Zitieren

Kottke T, Batschauer A, Ahmad M, Heberle J. Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry. 2006;45(8):2472-2479.
Kottke, T., Batschauer, A., Ahmad, M., & Heberle, J. (2006). Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry, 45(8), 2472-2479. https://doi.org/10.1021/bi051964b
Kottke, Tilman, Batschauer, Alfred, Ahmad, Margaret, and Heberle, Joachim. 2006. “Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy”. Biochemistry 45 (8): 2472-2479.
Kottke, T., Batschauer, A., Ahmad, M., and Heberle, J. (2006). Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry 45, 2472-2479.
Kottke, T., et al., 2006. Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry, 45(8), p 2472-2479.
T. Kottke, et al., “Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy”, Biochemistry, vol. 45, 2006, pp. 2472-2479.
Kottke, T., Batschauer, A., Ahmad, M., Heberle, J.: Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry. 45, 2472-2479 (2006).
Kottke, Tilman, Batschauer, Alfred, Ahmad, Margaret, and Heberle, Joachim. “Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy”. Biochemistry 45.8 (2006): 2472-2479.

45 Zitationen in Europe PMC

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Proton transfer to flavin stabilizes the signaling state of the blue light receptor plant cryptochrome.
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Quantifying electron transfer reactions in biological systems: what interactions play the major role?
Sjulstok E, Olsen JM, Solov'yov IA., Sci Rep 5(), 2015
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Separation of photo-induced radical pair in cryptochrome to a functionally critical distance.
Solov'yov IA, Domratcheva T, Schulten K., Sci Rep 4(), 2014
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A novel cryptochrome in the diatom Phaeodactylum tricornutum influences the regulation of light-harvesting protein levels.
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Observation of magnetic field effects on transient fluorescence spectra of cryptochrome 1 from homing pigeons.
Du XL, Wang J, Pan WS, Liu QJ, Wang XJ, Wu WJ., Photochem Photobiol 90(5), 2014
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ATP binding turns plant cryptochrome into an efficient natural photoswitch.
Müller P, Bouly JP, Hitomi K, Balland V, Getzoff ED, Ritz T, Brettel K., Sci Rep 4(), 2014
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Optogenetic control of cell function using engineered photoreceptors.
Pathak GP, Vrana JD, Tucker CL., Biol Cell 105(2), 2013
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A radical sense of direction: signalling and mechanism in cryptochrome magnetoreception.
Dodson CA, Hore PJ, Wallace MI., Trends Biochem Sci 38(9), 2013
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Magnetic field effects in flavoproteins and related systems.
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Reaction kinetics and mechanism of magnetic field effects in cryptochrome.
Solov'yov IA, Schulten K., J Phys Chem B 116(3), 2012
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A flavin binding cryptochrome photoreceptor responds to both blue and red light in Chlamydomonas reinhardtii.
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Fourier-transform infrared study of the photoactivation process of Xenopus (6-4) photolyase.
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Single amino acid substitution reveals latent photolyase activity in Arabidopsis cry1.
Burney S, Wenzel R, Kottke T, Roussel T, Hoang N, Bouly JP, Bittl R, Heberle J, Ahmad M., Angew Chem Int Ed Engl 51(37), 2012
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Decrypting cryptochrome: revealing the molecular identity of the photoactivation reaction.
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The cryptochromes: blue light photoreceptors in plants and animals.
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Indication for a radical intermediate preceding the signaling state in the LOV domain photocycle.
Bauer C, Rabl CR, Heberle J, Kottke T., Photochem Photobiol 87(3), 2011
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Introduction to the Symposium-in Print: Blue light effects.
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Light-regulated interactions with SPA proteins underlie cryptochrome-mediated gene expression.
Fankhauser C, Ulm R., Genes Dev 25(10), 2011
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Light-induced conformational changes in full-length Arabidopsis thaliana cryptochrome.
Kondoh M, Shiraishi C, Müller P, Ahmad M, Hitomi K, Getzoff ED, Terazima M., J Mol Biol 413(1), 2011
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Photoexcitation of the blue light using FAD photoreceptor AppA results in ultrafast changes to the protein matrix.
Lukacs A, Haigney A, Brust R, Zhao RK, Stelling AL, Clark IP, Towrie M, Greetham GM, Meech SR, Tonge PJ., J Am Chem Soc 133(42), 2011
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The Electronic State of Flavoproteins: Investigations with Proton Electron-Nuclear Double Resonance.
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Key dynamics of conserved asparagine in a cryptochrome/photolyase family protein by fourier transform infrared spectroscopy.
Iwata T, Zhang Y, Hitomi K, Getzoff ED, Kandori H., Biochemistry 49(41), 2010
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Functional motifs in the (6-4) photolyase crystal structure make a comparative framework for DNA repair photolyases and clock cryptochromes.
Hitomi K, DiTacchio L, Arvai AS, Yamamoto J, Kim ST, Todo T, Tainer JA, Iwai S, Panda S, Getzoff ED., Proc Natl Acad Sci U S A 106(17), 2009
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Photocycle dynamics of the E149A mutant of cryptochrome 3 from Arabidopsis thaliana.
Zirak P, Penzkofer A, Moldt J, Pokorny R, Batschauer A, Essen LO., J Photochem Photobiol B 97(2), 2009
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Role of exchange and dipolar interactions in the radical pair model of the avian magnetic compass.
Efimova O, Hore PJ., Biophys J 94(5), 2008
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Human and Drosophila cryptochromes are light activated by flavin photoreduction in living cells.
Hoang N, Schleicher E, Kacprzak S, Bouly JP, Picot M, Wu W, Berndt A, Wolf E, Bittl R, Ahmad M., PLoS Biol 6(7), 2008
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Cryptochrome 3 from Arabidopsis thaliana: structural and functional analysis of its complex with a folate light antenna.
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Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii.
Song SH, Dick B, Penzkofer A, Hegemann P., J Photochem Photobiol B 87(1), 2007
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Losi A., Photochem Photobiol 83(6), 2007
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Absorption and fluorescence spectroscopic characterization of cryptochrome 3 from Arabidopsis thaliana.
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