scholarly journals In Vivo Identification of Photosystem II Light Harvesting Complexes Interacting with PHOTOSYSTEM II SUBUNIT S

2015 ◽  
Vol 168 (4) ◽  
pp. 1747-1761 ◽  
Author(s):  
Caterina Gerotto ◽  
Cinzia Franchin ◽  
Giorgio Arrigoni ◽  
Tomas Morosinotto
Keyword(s):  
Photosystem Ii ◽  
Light Harvesting ◽  
Light Harvesting Complexes

scholarly journals Identification of parallel pH- and zeaxanthin-dependent quenching of excess energy in LHCSR3 in Chlamydomonas reinhardtii

2020 ◽  
Author(s):  
Julianne M. Troiano ◽  
Federico Perozeni ◽  
Raymundo Moya ◽  
Luca Zuliani ◽  
Kwangryul Baek ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Light Harvesting ◽  
Complex Stress ◽  
Excess Energy ◽  
Photochemical Quenching ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Non Photochemical Quenching

AbstractUnder high light conditions, oxygenic photosynthetic organisms avoid photodamage by thermally dissipating excess absorbed energy, which is called non-photochemical quenching (NPQ). In green algae, a chlorophyll and carotenoid-binding protein, light-harvesting complex stress-related (LHCSR3), detects excess energy via pH and serves as a quenching site. However, the mechanisms by which LHCSR3 functions have not been determined. Using a combined in vivo and in vitro approach, we identify two parallel yet distinct quenching processes, individually controlled by pH and carotenoid composition, and their likely molecular origin within LHCSR3 from Chlamydomonas reinhardtii. The pH-controlled quenching is removed within a mutant LHCSR3 that lacks the protonable residues responsible for sensing pH. Constitutive quenching in zeaxanthin-enriched systems demonstrates zeaxanthin-controlled quenching, which may be shared with other light-harvesting complexes. We show that both quenching processes prevent the formation of damaging reactive oxygen species, and thus provide distinct timescales and mechanisms of protection in a changing environment.

scholarly journals Determination of the Stoichiometry and Strength of Binding of Xanthophylls to the Photosystem II Light Harvesting Complexes

1999 ◽  
Vol 274 (15) ◽  
pp. 10458-10465 ◽  
Author(s):  
Alexander V. Ruban ◽  
Pamela J. Lee ◽  
Mark Wentworth ◽  
Andrew J. Young ◽  
Peter Horton
Keyword(s):  
Photosystem Ii ◽  
Light Harvesting ◽  
Light Harvesting Complexes

scholarly journals From isolated light-harvesting complexes to the thylakoid membrane: a single-molecule perspective

Nanophotonics ◽  
2018 ◽  
Vol 7 (1) ◽  
pp. 81-92 ◽  
Author(s):  
J. Michael Gruber ◽  
Pavel Malý ◽  
Tjaart P.J. Krüger ◽  
Rienk van Grondelle
Keyword(s):  
Single Molecule ◽  
Thylakoid Membrane ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Conformational Dynamics ◽  
Physical Models ◽  
Photochemical Quenching ◽  
Light Harvesting Complexes ◽  
Fluorescence Measurements

AbstractThe conversion of solar radiation to chemical energy in plants and green algae takes place in the thylakoid membrane. This amphiphilic environment hosts a complex arrangement of light-harvesting pigment-protein complexes that absorb light and transfer the excitation energy to photochemically active reaction centers. This efficient light-harvesting capacity is moreover tightly regulated by a photoprotective mechanism called non-photochemical quenching to avoid the stress-induced destruction of the catalytic reaction center. In this review we provide an overview of single-molecule fluorescence measurements on plant light-harvesting complexes (LHCs) of varying sizes with the aim of bridging the gap between the smallest isolated complexes, which have been well-characterized, and the native photosystem. The smallest complexes contain only a small number (10–20) of interacting chlorophylls, while the native photosystem contains dozens of protein subunits and many hundreds of connected pigments. We discuss the functional significance of conformational dynamics, the lipid environment, and the structural arrangement of this fascinating nano-machinery. The described experimental results can be utilized to build mathematical-physical models in a bottom-up approach, which can then be tested on larger in vivo systems. The results also clearly showcase the general property of biological systems to utilize the same system properties for different purposes. In this case it is the regulated conformational flexibility that allows LHCs to switch between efficient light-harvesting and a photoprotective function.

Control of plant growth and water loss by a lack of light-harvesting complexes in photosystem II in Arabidopsis thaliana ch1-1 mutant

2014 ◽  
Vol 36 (7) ◽  
pp. 1627-1635 ◽  
Author(s):  
Md Sarwar Jahan ◽  
Mohd Nozulaidi ◽  
Mohammad Moneruzzaman Khandaker ◽  
Ainun Afifah ◽  
Nurul Husna
Keyword(s):  
Arabidopsis Thaliana ◽  
Photosystem Ii ◽  
Plant Growth ◽  
Water Loss ◽  
Light Harvesting ◽  
Light Harvesting Complexes

scholarly journals Allosteric regulation of the light-harvesting system of photosystem II

2000 ◽  
Vol 355 (1402) ◽  
pp. 1361-1370 ◽  
Author(s):  
Peter Horton ◽  
Alexander V. Ruban ◽  
Mark Wentworth
Keyword(s):  
Photosystem Ii ◽  
Xanthophyll Cycle ◽  
Light Harvesting ◽  
Allosteric Regulation ◽  
Photochemical Quenching ◽  
Protein Subunit ◽  
Ps Ii ◽  
Non Photochemical Quenching

Non–photochemical quenching of chlorophyll fluorescence (NPQ) is symptomatic of the regulation of energy dissipation by the light–harvesting antenna of photosystem II (PS II). The kinetics of NPQ in both leaves and isolated chloroplasts are determined by the transthylakoid ΔpH and the de–epoxidation state of the xanthophyll cycle. In order to understand the mechanism and regulation of NPQ we have adopted the approaches commonly used in the study of enzyme–catalysed reactions. Steady–state measurements suggest allosteric regulation of NPQ, involving control by the xanthophyll cycle carotenoids of a protonationdependent conformational change that transforms the PS II antenna from an unquenched to a quenched state. The features of this model were confirmed using isolated light–harvesting proteins. Analysis of the rate of induction of quenching both in vitro and in vivo indicated a bimolecular second–order reaction; it is suggested that quenching arises from the reaction between two fluorescent domains, possibly within a single protein subunit. A universal model for this transition is presented based on simple thermodynamic principles governing reaction kinetics.

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