scholarly journals Size and Fluorescence Properties of Algal Photosynthetic Antenna Proteins Estimated by Microscopy

2022 ◽  
Vol 23 (2) ◽  
pp. 778
Author(s):  
Aurélie Crepin ◽  
Erica Belgio ◽  
Barbora Šedivá ◽  
Eliška Kuthanová Trsková ◽  
Edel Cunill-Semanat ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Higher Plants ◽  
Correlation Spectroscopy ◽  
Experimental Conditions ◽  
Light Harvesting Complex ◽  
Light Harvesting Complex Ii ◽  
Particle Level ◽  
Antenna Proteins ◽  
Photosynthetic Antenna

Antenna proteins play a major role in the regulation of light-harvesting in photosynthesis. However, less is known about a possible link between their sizes (oligomerization state) and fluorescence intensity (number of photons emitted). Here, we used a microscopy-based method, Fluorescence Correlation Spectroscopy (FCS), to analyze different antenna proteins at the particle level. The direct comparison indicated that Chromera Light Harvesting (CLH) antenna particles (isolated from Chromera velia) behaved as the monomeric Light Harvesting Complex II (LHCII) (from higher plants), in terms of their radius (based on the diffusion time) and fluorescence yields. FCS data thus indicated a monomeric oligomerization state of algal CLH antenna (at our experimental conditions) that was later confirmed also by biochemical experiments. Additionally, our data provide a proof of concept that the FCS method is well suited to measure proteins sizes (oligomerization state) and fluorescence intensities (photon counts) of antenna proteins per single particle (monomers and oligomers). We proved that antenna monomers (CLH and LHCIIm) are more “quenched” than the corresponding trimers. The FCS measurement thus represents a useful experimental approach that allows studying the role of antenna oligomerization in the mechanism of photoprotection.

scholarly journals Xanthophylls in Light-Harvesting Complex II of Higher Plants:  Light Harvesting and Triplet Quenching†

Biochemistry ◽  
1997 ◽  
Vol 36 (40) ◽  
pp. 12208-12215 ◽  
Author(s):  
Erwin J. G. Peterman ◽  
Claudiu C. Gradinaru ◽  
Florentine Calkoen ◽  
Jeroen C. Borst ◽  
Rienk van Grondelle ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Higher Plants ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Light Harvesting Complex Ii

scholarly journals Chlorophyll a and carotenoid triplet states in light-harvesting complex II of higher plants

1995 ◽  
Vol 69 (6) ◽  
pp. 2670-2678 ◽  
Author(s):  
E.J. Peterman ◽  
F.M. Dukker ◽  
R. van Grondelle ◽  
H. van Amerongen
Keyword(s):  
Chlorophyll A ◽  
Light Harvesting ◽  
Higher Plants ◽  
Triplet States ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Light Harvesting Complex Ii

Ultrafast Spectroscopy of Trimeric Light-Harvesting Complex II from Higher Plants

1997 ◽  
Vol 101 (10) ◽  
pp. 1902-1909 ◽  
Author(s):  
J. P. Connelly ◽  
M. G. Müller ◽  
M. Hucke ◽  
G. Gatzen ◽  
C. W. Mullineaux ◽  
...  
Keyword(s):  
Ultrafast Spectroscopy ◽  
Light Harvesting ◽  
Higher Plants ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Light Harvesting Complex Ii

scholarly journals Observation of dissipative chlorophyll-to-carotenoid energy transfer in light-harvesting complex II in membrane nanodiscs

2019 ◽  
Author(s):  
Minjung Son ◽  
Alberta Pinnola ◽  
Samuel C. Gordon ◽  
Roberto Bassi ◽  
Gabriela S. Schlau-Cohen
Keyword(s):  
Energy Transfer ◽  
Conformational Changes ◽  
Light Harvesting ◽  
Electronic Spectroscopy ◽  
Local Environment ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Light Harvesting Complex Ii ◽  
Photosynthetic Antenna

<pre><p><a></a>Green plants prevent photodamage under high light conditions by dissipating excess energy as heat. Conformational changes of the photosynthetic antenna complexes activate dissipation by leveraging the sensitivity of the photophysics of the chlorophyll and carotenoids to their surrounding protein. However, the mechanisms and site of dissipation are still debated, largely due to two challenges. First, because of the ultrafast timescales and large energy gaps involved, measurements lacked the temporal or spectral requirements. Second, experiments have been performed in detergent, which can induce non-native conformations, or <i>in vivo</i>, where contributions from the multiple complexes cannot be disentangled and are further obfuscated by laser-induced artifacts. Here, we overcome both challenges by applying ultrabroadband two-dimensional electronic spectroscopy to the principal antenna complex, light-harvesting complex II, in a near-native membrane. The membrane enhances two dissipative pathways, one of which was previously uncharacterized chlorophyll-to-carotenoid energy transfer. Our results highlight the sensitivity of the photophysics to the local environment, which may be used to control the balance between light harvesting and dissipation <i>in vivo</i>.</p></pre>

The structure of the Physcomitrium Patens Photosystem I Reveals a Unique Lhca2 Paralogue replacing Lhca4

2021 ◽  
Author(s):  
Yuval Mazor ◽  
Christopher Gorski ◽  
Reece Riddle ◽  
Hila Toporik ◽  
Zhen Da ◽  
...  
Keyword(s):  
Photosystem I ◽  
Light Harvesting ◽  
Higher Plants ◽  
Algal Species ◽  
Low Light ◽  
Light Harvesting Complex ◽  
Light Harvesting Complex Ii ◽  
Ancient Plants ◽  
Colonization Of Land ◽  
Green Lineage

The moss Physcomitrium patens diverged from green algae shortly after the colonization of land by ancient plants. This colonization posed new environmental challenges which drove evolutionary processes. The photosynthetic machinery of modern flowering plants is adapted to the high light conditions on land. Red shifted Lhca4 antennae are present in the photosystem I light harvesting complex of many green lineage plants but absent from P. patens. The Cryo-EM structure of the P. patens photosystem I light harvesting complex I supercomplex (PSI-LHCI) at 2.8 Å reveals that Lhca4 is replaced by a unique Lhca2 paralogue in moss. This PSI-LHCI supercomplex also retains the PsaM subunit, present in cyanobacteria and several algal species but lost in higher plants, and the PsaO subunit responsible for binding light harvesting complex II. The blue shifted Lhca2 paralogue and chlorophyll b enrichment relative to higher plants make the P. patens PSI-LHCI spectroscopically unique among other green lineage supercomplexes. Overall, the structure represents an evolutionary intermediate PSI with the crescent shaped LHCI common in higher plants and contains a unique Lhca2 paralogue which facilitates the mosses adaptation to low light niches.

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