Please use this identifier to cite or link to this item:
Title: Energizing the light harvesting antenna: Insight from CP29
Authors: Ioannidis, Nikolaos E. 
Papadatos, Sotiris 
Daskalakis, Vangelis 
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

CORE Recommender
Show full item record

Citations 10

checked on May 31, 2020

Page view(s) 10

Last Week
Last month
checked on Jun 1, 2020

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.