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|Title:||Energizing the light harvesting antenna: Insight from CP29||Authors:||Ioannidis, Nikolaos E.
|Keywords:||Antenna proteins;Non photochemical quenching;Photoprotection;Photosystem II;Proton motive force||Category:||Other Agricultural Sciences||Field:||Agricultural Sciences||Issue Date:||1-Oct-2016||Publisher:||Elsevier||Source:||Biochimica et Biophysica Acta - Bioenergetics, 2016, vol. 1857, no. 10, pp. 1643-1650||Journal:||Biochimica et Biophysica Acta - Bioenergetics||Abstract:||How do plants cope with excess light energy? Crop health and stress tolerance are governed by molecular photoprotective mechanisms. Protective exciton quenching in plants is activated by membrane energization, via unclear conformational changes in proteins called antennas. Here we show that pH and salt gradients stimulate the response of such an antenna under low and high energization by all-atom Molecular Dynamics Simulations. Novel insight establishes that helix-5 (H5) conformation in CP29 from spinach is regulated by chemiosmotic factors. This is selectively correlated with the chl-614 macrocycle deformation and interactions with nearby pigments, that could suggest a role in plant photoprotection. Adding to the significance of our findings, H5 domain is conserved among five antennas (LHCB1–5). These results suggest that light harvesting complexes of Photosystem II, one of the most abundant proteins on earth, can sense chemiosmotic gradients via their H5 domains in an upgraded role from a solar detector to also a chemiosmotic sensor.||ISSN:||0005-2728||DOI:||10.1016/j.bbabio.2016.07.005||Collaboration :||Cyprus University of Technology||Rights:||© Elsevier||Type:||Article|
|Appears in Collections:||Άρθρα/Articles|
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