Light-harvesting chlorophyll a-b complex requirement for regulation of Photosystem II photochemistry by non-photochemical quenching

1994 ◽  
Vol 40 (3) ◽  
pp. 287-294 ◽  
Author(s):  
Jean-Marie Briantais
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Light Harvesting ◽  
Photochemical Quenching ◽  
Photosystem Ii Photochemistry ◽  
Non Photochemical Quenching

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.

Regulation of Non-Photochemical Quenching of Chlorophyll Fluorescence in Plants

1995 ◽  
Vol 22 (2) ◽  
pp. 221 ◽  
Author(s):  
AV Ruban ◽  
P Horton
Keyword(s):  
Chlorophyll Fluorescence ◽  
Photosystem Ii ◽  
Excited States ◽  
Light Harvesting ◽  
Structure And Function ◽  
Photochemical Quenching ◽  
Dynamic Nature ◽  
Dissipation Of Energy ◽  
And Function ◽  
Non Photochemical Quenching

Non-photochemical quenching of chlorophyll fluorescence indicates the de-excitation of light-generated excited states in the chlorophyll associated with photosystem II (PSII). The principle process contributing to this quenching is dependent on the formation of the thylakoid proton gradient and is an important mechanism for protecting PSII from photodamage. Evidence points to the importance of the light-harvesting chlorophyll proteins as the site of dissipation of energy, and suggests that the structure and function of these proteins are regulated by protonation and the ratio of zeaxanthin to violaxanthin. The minor light-harvesting proteins may have a particularly important role as the primary sites of proton binding and because of their enrichment in xanthophyll cycle carotenoids. The dynamic nature of the light-harvesting system is an important part of the process by which plants are able to adapt to different light environments.

scholarly journals The carotenoid pathway: what is important for excitation quenching in plant antenna complexes?

2017 ◽  
Vol 19 (34) ◽  
pp. 22957-22968 ◽  
Author(s):  
Kieran F. Fox ◽  
Vytautas Balevičius ◽  
Jevgenij Chmeliov ◽  
Leonas Valkunas ◽  
Alexander V. Ruban ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Excitation Energy ◽  
Light Harvesting ◽  
High Light ◽  
Photochemical Quenching ◽  
Non Photochemical Quenching ◽  
Carotenoid Pathway

Plant light-harvesting is regulated by the Non-Photochemical Quenching (NPQ) mechanism involving the slow trapping of excitation energy by carotenoids in the Photosystem II (PSII) antenna in response to high light.

scholarly journals Towards spruce-type photosystem II: consequences of the loss of light-harvesting proteins LHCB3 and LHCB6 in Arabidopsis

2021 ◽  
Author(s):  
Iva Ilíková ◽  
Petr Ilík ◽  
Monika Opatíková ◽  
Rameez Arshad ◽  
Lukáš Nosek ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Light Harvesting ◽  
Light Exposure ◽  
Land Plants ◽  
Photochemical Quenching ◽  
Functional Changes ◽  
Electron Microscopy Analysis ◽  
Function Characterization ◽  
Microscopy Analysis ◽  
Non Photochemical Quenching

Abstract The largest stable photosystem II (PSII) supercomplex in land plants (C2S2M2) consists of a core complex dimer (C2), two strongly (S2) and two moderately (M2) bound light-harvesting protein (LHCB) trimers attached to C2 via monomeric antenna proteins LHCB4–6. Recently, we have shown that LHCB3 and LHCB6, presumably essential for land plants, are missing in Norway spruce (Picea abies), which results in a unique structure of its C2S2M2 supercomplex. Here, we performed structure–function characterization of PSII supercomplexes in Arabidopsis (Arabidopsis thaliana) mutants lhcb3, lhcb6, and lhcb3 lhcb6 to examine the possibility of the formation of the “spruce-type” PSII supercomplex in angiosperms. Unlike in spruce, in Arabidopsis both LHCB3 and LHCB6 are necessary for stable binding of the M trimer to PSII core. The “spruce-type” PSII supercomplex was observed with low abundance only in the lhcb3 plants and its formation did not require the presence of LHCB4.3, the only LHCB4-type protein in spruce. Electron microscopy analysis of grana membranes revealed that the majority of PSII in lhcb6 and namely in lhcb3 lhcb6 mutants were arranged into C2S2 semi-crystalline arrays, some of which appeared to structurally restrict plastoquinone diffusion. Mutants without LHCB6 were characterized by fast induction of non-photochemical quenching and, on the contrary to the previous lhcb6 study, by only transient slowdown of electron transport between PSII and PSI. We hypothesize that these functional changes, associated with the arrangement of PSII into C2S2 arrays in thylakoids, may be important for the photoprotection of both PSI and PSII upon abrupt high-light exposure.

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.

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