Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins

Immeln D, Pokorny R, Herman E, Moldt J, Batschauer A, Kottke T (2010)
Journal of Physical Chemistry B 114(51): 17155-17161.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Journal of Physical Chemistry B
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114
Zeitschriftennummer
51
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17155-17161
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Immeln D, Pokorny R, Herman E, Moldt J, Batschauer A, Kottke T. Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins. Journal of Physical Chemistry B. 2010;114(51):17155-17161.
Immeln, D., Pokorny, R., Herman, E., Moldt, J., Batschauer, A., & Kottke, T. (2010). Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins. Journal of Physical Chemistry B, 114(51), 17155-17161. doi:10.1021/jp1076388
Immeln, D., Pokorny, R., Herman, E., Moldt, J., Batschauer, A., and Kottke, T. (2010). Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins. Journal of Physical Chemistry B 114, 17155-17161.
Immeln, D., et al., 2010. Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins. Journal of Physical Chemistry B, 114(51), p 17155-17161.
D. Immeln, et al., “Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins”, Journal of Physical Chemistry B, vol. 114, 2010, pp. 17155-17161.
Immeln, D., Pokorny, R., Herman, E., Moldt, J., Batschauer, A., Kottke, T.: Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins. Journal of Physical Chemistry B. 114, 17155-17161 (2010).
Immeln, Dominik, Pokorny, Richard, Herman, Elena, Moldt, Julia, Batschauer, Alfred, and Kottke, Tilman. “Photoreaction of Plant and DASH Cryptochromes Probed by Infrared Spectroscopy: The Neutral Radical State of Flavoproteins”. Journal of Physical Chemistry B 114.51 (2010): 17155-17161.

8 Zitationen in Europe PMC

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Signaling mechanisms of plant cryptochromes in Arabidopsis thaliana.
Liu B, Yang Z, Gomez A, Liu B, Lin C, Oka Y., J Plant Res 129(2), 2016
PMID: 26810763
Proton transfer to flavin stabilizes the signaling state of the blue light receptor plant cryptochrome.
Hense A, Herman E, Oldemeyer S, Kottke T., J Biol Chem 290(3), 2015
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A novel cryptochrome in the diatom Phaeodactylum tricornutum influences the regulation of light-harvesting protein levels.
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PMID: 24898692
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PMID: 23938034
Decrypting cryptochrome: revealing the molecular identity of the photoactivation reaction.
Solov'yov IA, Domratcheva T, Moughal Shahi AR, Schulten K., J Am Chem Soc 134(43), 2012
PMID: 23009093
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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