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Dynamic Nuclear Polarization Provides New Insights into Chromophore Structure in Phytochrome Photoreceptors
Citation key ANGE:ANGE201608119
Author Stöppler, Daniel and Song, Chen and van Rossum, Barth-Jan and Geiger, Michel-Andreas and Lang, Christina and Mroginski, Maria-Andrea and Jagtap, Anil Pandurang and Sigurdsson, Snorri Th. and Matysik, Jörg and Hughes, Jon and Oschkinat, Hartmut
Pages 16251–16254
Year 2016
ISSN 1521-3757
DOI 10.1002/ange.201608119
Journal Angewandte Chemie
Volume 128
Number 52
Abstract Phytochromes are red/far-red photochromic photoreceptors acting as master regulators of development in higher plants, thereby controlling transcription of about 20 % of their genes. Light-induced isomerization of the bilin chromophore leads to large rearrangements in protein structure, whereby the role of protonation dynamics and charge distribution is of particular interest. To help unravel the inherent mechanisms, we present two-dimensional dynamic nuclear polarization (DNP) enhanced solid-state magic-angle spinning (MAS) NMR spectra of the functional sensory module of the cyanobacterial phytochrome Cph1. To this end, the pyrrole ring nitrogen signals were assigned unequivocally, enabling us to locate the positive charge of the phycocyanobilin (PCB) chromophore. To help analyze proton exchange pathways, the proximity of PCB ring nitrogen atoms and functionally relevant H2O molecules was also determined. Our study demonstrates the value of DNP in biological solid-state MAS NMR spectroscopy.
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