Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 476702
Title Conformational switching explains the intrinsic multifunctionality of plant light-harvesting complexes
Author(s) Kruger, T.P.; Wientjes, E.; Croce, R.; Grondelle, R. van
Source Proceedings of the National Academy of Sciences of the United States of America 108 (2011)33. - ISSN 0027-8424 - p. 13516 - 13521.
DOI https://doi.org/10.1073/pnas.1105411108
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) pigment-pigment interactions - energy transfer pathways - charge-transfer state - single lh2 complexes - far-red fluorescence - photosystem-i - antenna complexes - angstrom resolution - protein complexes - crystal-structure
Abstract The light-harvesting complexes of photosystem I and II (Lhcas and Lhcbs) of plants display a high structural homology and similar pigment content and organization. Yet, the spectroscopic properties of these complexes, and accordingly their functionality, differ substantially. This difference is primarily due to the charge-transfer (CT) character of a chlorophyll dimer in all Lhcas, which mixes with the excitonic states of these complexes, whereas this CT character is generally absent in Lhcbs. By means of single-molecule spectroscopy near room temperature, we demonstrate that the presence or absence of such a CT state in Lhcas and Lhcbs can occasionally be reversed; i.e., these complexes are able to interconvert conformationally to quasi-stable spectral states that resemble the Lhcs of the other photosystem. The high structural similarity of all the Lhca and Lhcb proteins suggests that the stable conformational states that give rise to the mixed CT-excitonic state are similar for all these proteins, and similarly for the conformations that involve no CT state. This indicates that the specific functions related to Lhca and Lhcb complexes are realized by different stable conformations of a single generic protein structure. We propose that this functionality is modulated and controlled by the protein environment.
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