The major trimeric antenna complexes serve as a site for qH-energy dissipation in plants

Bru, Pierrick; Steen, Collin J.; Park, Sumin; Amstutz, Cynthia L.; Sylak-Glassman, Emily J.; Lam, Lam; Fekete, Ágnes; Mueller, Martin J.; Longoni, Paolo; Fleming, Graham R.; Niyogi, Krishna; Malnoë, Alizée

doi:10.1016/j.jbc.2022.102519

Cited by 10 publications

(6 citation statements)

References 75 publications

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“…Bru et al showed that the qH quenching site is a major trimeric antenna complex composed of Lhcb1, Lhcb2 and Lhcb3, which can form homotrimeric and heterotrimeric complexes. Interestingly, a specific subunit of the major trimeric antenna complex is not required for qH induction (Bru et al, 2022).…”

Section: A Model For the Role Of Lumenal Redox Regulation In Photopro...mentioning

confidence: 99%

“…qH is known to be redox‐regulated but independent of protonation of PsbS, accumulation of Zx and phosphorylation by STN7 (Brooks et al, 2013; Bru et al, 2022; Malnoë, Schultink, et al, 2018). It has been shown that qH is induced by oxidative stress conditions such as cold and high light (Brooks et al, 2013; Bru et al, 2022; Levesque‐Tremblay et al, 2009; Malnoë, Schultink, et al, 2018).…”

Section: A Model For the Role Of Lumenal Redox Regulation In Photopro...mentioning

confidence: 99%

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Redox regulation in chloroplast thylakoid lumen: The pmf changes everything, again

Hoh,

Froehlich,

Kramer

2023

Plant Cell & Environment

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Photosynthesis is the foundation of life on Earth. However, if not well regulated, it can also generate excessive reactive oxygen species (ROS), which can cause photodamage. Regulation of photosynthesis is highly dynamic, responding to both environmental and metabolic cues, and occurs at many levels, from light capture to energy storage and metabolic processes. One general mechanism of regulation involves the reversible oxidation and reduction of protein thiol groups, which can affect the activity of enzymes and the stability of proteins. Such redox regulation has been well studied in stromal enzymes, but more recently, evidence has emerged of redox control of thylakoid lumenal enzymes. This review/hypothesis paper summarizes the latest research and discusses several open questions and challenges to achieving effective redox control in the lumen, focusing on the distinct environments and regulatory components of the thylakoid lumen, including the need to transport electrons across the thylakoid membrane, the effects of pH changes by the proton motive force (pmf) in the stromal and lumenal compartments, and the observed differences in redox states. These constraints suggest that activated oxygen species are likely to be major regulatory contributors to lumenal thiol redox regulation, with key components and processes yet to be discovered.

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Section: A Model For the Role Of Lumenal Redox Regulation In Photopro...mentioning

confidence: 99%

Section: A Model For the Role Of Lumenal Redox Regulation In Photopro...mentioning

confidence: 99%

Redox regulation in chloroplast thylakoid lumen: The pmf changes everything, again

Hoh,

Froehlich,

Kramer

2023

Plant Cell & Environment

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“…LHCII is found in the chloroplast thylakoid membrane of eukaryotic photosynthetic organisms. LHCII is a homotrimeric or heterotrimeric pigment–protein complex that is associated weakly and strongly with PSII − in a PSII–LHCII supercomplex . The individual monomers of LHCII are encoded by the lhcb gene family and are well conserved across species.…”

Section: Introductionmentioning

confidence: 99%

Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II

Ranepura,

Mao,

Vermaas

et al. 2023

J. Phys. Chem. B

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“…LHCII form homotrimeric or heterotrimeric pigment-protein complexes that are associated to PSII ranging from a strongly to an insecurely bound manner [15][16][17]. LHCII is found in the chloroplast thylakoid membrane of eukaryotic photosynthetic organisms in a PSII-LHCII supercomplex [18].…”

Section: Introductionmentioning

confidence: 99%

Computing the relative affinity of chlorophylls a and b to light-harvesting complex II

Ranepura,

Mao,

Vermaas

et al. 2023

Preprint

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In plants and algae, the primary antenna protein bound to photosystem II is light harvesting complex II (LHCII), a pigment-protein complex that binds both chlorophyll (Chl) a and Chl b molecules. Chl a and Chl b have similar structures but differ in the chemical composition of their side chains. Chl a has a methyl group (-CH₃) on one of its pyrrole rings, while Chl b has a formyl group (-CHO) in the same position. There are 14 Chl binding sites but it is not known how the protein selectively binds the right chlorophyll type in each site. Knowing the selection criteria would allow the design of light harvesting complexes which bind different Chl types allowing an organism to utilize light of different wavelengths. The difference in the binding affinity of Chl a and Chl b in pea and spinach LHCII was calculated using Multiconformation Continuum Electrostatics and Free Energy Perturbation. Both methods identify some Chl sites where the Chl type (a or b) bound has significantly higher affinity, especially when the protein provides a hydrogen bond for the Chl b formyl group. However, the Chl a sites often have little calculated preference for one Chl type, so they are predicted to bind a mixture of Chl a and b. Therefore, the electron density of the spinach LHCII was reanalyzed, confirming there is negligible Chl b in the Chl a binding sites. It is suggested that the protein chooses the correct Chl type during folding, segregating the preferred Chl to the correct binding site.

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The major trimeric antenna complexes serve as a site for qH-energy dissipation in plants

Cited by 10 publications

References 75 publications

Redox regulation in chloroplast thylakoid lumen: The pmf changes everything, again

Redox regulation in chloroplast thylakoid lumen: The pmf changes everything, again

Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II

Computing the relative affinity of chlorophylls a and b to light-harvesting complex II

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