Antenna arrangement and energy transfer pathways of a green algal photosystem-I–LHCI supercomplex

Su, Xiaodong; Ma, Jun; Pan, Xiaowei; Zhao, Xuelin; Chang, Wenrui; Liu, Zhenfeng; Zhang, Xinzheng; Li, Mei

doi:10.1038/s41477-019-0380-5

Cited by 130 publications

(110 citation statements)

References 48 publications

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“…These deviations may result from the different lengths of the FCP polypeptides and their distinctly different locations, which may confer them different roles in energy harvesting and transfer. A similar situation can be found in LHCII and LHCI in the green lineage organisms, where different numbers of Chls a and b , and slightly different bindings sites of Chls, are also found .…”

Section: Binding Features Of Chlorophylls and Carotenoids In Fcpssupporting

confidence: 73%

“…To understand the oligomeric state, organization of protein subunits, and the exact composition and distribution of pigments and other cofactors in the PSII core and its complex with antenna proteins, several PSII structures from cyanobacteria, red alga, green alga, and higher plants have been solved by cryo‐electron microscopy (cryo‐EM) and X‐ray crystallography . In particular, single‐particle cryo‐EM analysis has provided a powerful tool to unravel the organization of several PSII–LHC and PSI–LHC supercomplexes from different lineages of organisms from cyanobacteria to green algae and higher plants . The structure of PSII–FCPII from diatoms, however, was solved only recently , and a high‐resolution crystal structure of an isolated FCP dimer was also reported recently .…”

Section: Introductionmentioning

confidence: 99%

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Structural features of the diatom photosystem II–light‐harvesting antenna complex

Wang

Zhao

et al. 2020

The FEBS Journal

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In photosynthesis, light energy is captured by pigments bound to light-harvesting antenna proteins (LHC) that then transfer the energy to the photosystem (PS) cores to initiate photochemical reactions. The LHC proteins surround the PS cores to form PS-LHC supercomplexes. In order to adapt to a wide range of light environments, photosynthetic organisms have developed a large variety of pigments and antenna proteins to utilize the light energy efficiently under different environments. Diatoms are a group of important eukaryotic algae and possess fucoxanthin (Fx) chlorophyll a/c proteins (FCP) as antenna which have exceptional capabilities of harvesting blue-green light under water and dissipate excess energy under strong light conditions. We have solved the structure of a PSII-FCPII supercomplex from a centric diatom Chaetoceros gracilis by cryo-electron microscopy, and also the structure of an isolated FCP dimer from a pennate diatom Phaeodactylum tricornutum by X-ray crystallography at a high resolution.These results revealed the oligomerization states of FCPs distinctly different from those of LHCII found in the green lineage organisms, the detailed binding patterns of Chl c and Fxs, a huge pigment network, and extensive protein-protein, pigment-protein, and pigment-pigment interactions within the PSII-FCPII supercomplex. These results therefore provide a solid structural basis for examining the detailed mechanisms of the highly efficient energy transfer and quenching processes in diatoms.

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Section: Binding Features Of Chlorophylls and Carotenoids In Fcpssupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Wang

Zhao

et al. 2020

The FEBS Journal

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“…To understand the molecular mechanisms of the light reactions, it is an invaluable asset to use a tool that can reconstruct the ensemble of possible conformations, reorganizations, interactions, and movements taking place within the thylakoid. In the past years, several high-resolution structures of the main photosynthetic complexes active in the first steps of photosynthesis (LHCs, PSII, and PSI) have been obtained via X-ray crystallography and cryo-electron microscopy (Pan et al 2011;Umena et al 2011;Fan et al 2015;Qin et al 2015Qin et al , 2019Wei et al 2016;Su et al 2017Su et al , 2019. These structures are in many cases a superposition of multiple conformations of these complexes and, therefore, lack information of the single states of the system.…”

Section: Introduction: Towards a Dynamic Structural View Of Photosyntmentioning

confidence: 99%

Molecular dynamics simulations in photosynthesis

Liguori¹,

Croce²,

Marrink

et al. 2020

Photosynth Res

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Photosynthesis is regulated by a dynamic interplay between proteins, enzymes, pigments, lipids, and cofactors that takes place on a large spatio-temporal scale. Molecular dynamics (MD) simulations provide a powerful toolkit to investigate dynamical processes in (bio)molecular ensembles from the (sub)picosecond to the (sub)millisecond regime and from the Å to hundreds of nm length scale. Therefore, MD is well suited to address a variety of questions arising in the field of photosynthesis research. In this review, we provide an introduction to the basic concepts of MD simulations, at atomistic and coarse-grained level of resolution. Furthermore, we discuss applications of MD simulations to model photosynthetic systems of different sizes and complexity and their connection to experimental observables. Finally, we provide a brief glance on which methods provide opportunities to capture phenomena beyond the applicability of classical MD.Publisher's Note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

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“…In the green alga Chlamydomonas reinhardtii , the LHCI antenna, which contains nine different Lhca proteins (Lhca1–9) (Busch and Hippler, ), is organized as a double row, with the more internal one in a similar position as Lhca1–4 in plants. Besides these Lhca, the binding of an additional dimer was recently described next to PsaH, PsaI, and PsaB, that is the side of the core complex opposite to the LHCII binding site (Ozawa et al , ; Suga et al , ; Su et al , ). A similar organization was also described in the green alga Bryopsis corticulans (Qin et al , ) as well as in the red alga Cyanidioschyzon merolae (Pi et al , ), suggesting that the binding site of this additional dimer is conserved among several photosynthetic organisms.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of a large photosystem I–light‐harvesting complex II supercomplex with an additional Lhca1–a4 dimer in Arabidopsis

et al. 2020

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The biological conversion of light energy into chemical energy is performed by a flexible photosynthetic machinery located in the thylakoid membranes. Photosystems I and II (PSI and PSII) are the two complexes able to harvest light. PSI is the last complex of the electron transport chain and is composed of multiple subunits: the proteins building the catalytic core complex that are well conserved between oxygenic photosynthetic organisms, and, in green organisms, the membrane light-harvesting complexes (Lhc) necessary to increase light absorption. In plants, four Lhca proteins (Lhca1-4) make up the antenna system of PSI, which can be further extended to optimize photosynthesis by reversible binding of LHCII, the main antenna complex of photosystem II. Here, we used biochemistry and electron microscopy in Arabidopsis to reveal a previously unknown supercomplex of PSI with LHCII that contains an additional Lhca1-a4 dimer bound on the PsaB-PsaI-PsaH side of the complex. This finding contradicts recent structural studies suggesting that the presence of an Lhca dimer at this position is an exclusive feature of algal PSI. We discuss the features of the additional Lhca dimer in the large plant PSI-LHCII supercomplex and the differences with the algal PSI. Our work provides further insights into the intricate structural plasticity of photosystems.

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Antenna arrangement and energy transfer pathways of a green algal photosystem-I–LHCI supercomplex

Cited by 130 publications

References 48 publications

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Structural features of the diatom photosystem II–light‐harvesting antenna complex

Molecular dynamics simulations in photosynthesis

Isolation and characterization of a large photosystem I–light‐harvesting complex II supercomplex with an additional Lhca1–a4 dimer in Arabidopsis

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