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Issue 2, 2015
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Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

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Abstract

Tryptophan residues at the dimer interface of the plant photoreceptor UVR8 promote monomerisation after UV-B absorption via a so far unknown mechanism. Using FTIR spectroscopy we assign light-induced structural transitions of UVR8 mainly to amino acid side chains without major transformations of the secondary structure of the physiologically relevant C-terminal extension. Additionally, we assign the monomerisation associated increase and red shift of the UVR8 tryptophan emission to a photoinduced rearrangement of tryptophan side chains and a relocation of the aspartic acid residues D96 and D107, respectively. By illumination dependent emission spectroscopy we furthermore determined the quantum yield of photoinduced monomerisation to 20 ± 8%.

Graphical abstract: Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

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Publication details

The article was received on 07 Jul 2014, accepted on 24 Sep 2014 and first published on 25 Sep 2014


Article type: Paper
DOI: 10.1039/C4PP00246F
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Citation: Photochem. Photobiol. Sci., 2015,14, 252-257

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    Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

    M. Heilmann, J. M. Christie, J. T. M. Kennis, G. I. Jenkins and T. Mathes, Photochem. Photobiol. Sci., 2015, 14, 252
    DOI: 10.1039/C4PP00246F

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