Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

Photosynthetic light-harvesting complexes (LHCs) of higher plants, moss, and green algae can undergo dynamic conformational transitions, which have been correlated to their ability to adapt to fluctuations in the light environment. Herein, we demonstrate the application of solid-state NMR spectroscopy on native, heterogeneous thylakoid membranes of Chlamydomonas reinhardtii (Cr) and on Cr light-harvesting complex II (LHCII) in thylakoid lipid bilayers to detect LHCII conformational dynamics in its native membrane environment. We show that membrane-reconstituted LHCII contains selective sites that undergo fast, large-amplitude motions, including the phytol tails of two chlorophylls. Protein plasticity is also observed in the N-terminal stromal loop and in protein fragments facing the lumen, involving sites that stabilize the xanthophyll-cycle carotenoid violaxanthin and the two luteins. The results report on the intrinsic flexibility of LHCII pigment-protein complexes in a membrane environment, revealing putative sites for conformational switching. In thylakoid membranes, fast dynamics of protein and pigment sites is significantly reduced, which suggests that in their native organelle membranes, LHCII complexes are locked in specific conformational states. Copyright © 2020 Biophysical Society. Published by Elsevier Inc. All rights reserved.


Fatemeh Azadi-Chegeni, Meaghan E Ward, Giorgio Perin, Diana Simionato, Tomas Morosinotto, Marc Baldus, Anjali Pandit. Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment. Biophysical journal. 2021 Jan 19;120(2):270-283

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 33285116

View Full Text