Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex

Gisriel, Christopher J.; Zhou, Kaifeng; Huang, Hao Li; Debus, Richard J.; Xiong, Yong; Brudvig, Gary W.

doi:10.1016/j.joule.2020.07.016

Cited by 44 publications

(75 citation statements)

References 92 publications

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“…The D1 C-terminus follows a different trajectory compared to the mature PSII. Thus, we provide structural evidence that the slow dark-rearrangement involves a conformational change of the D1 C-terminus rather than the previously proposed disorder-to-order transition after initial photoactivation (Gisriel et al, 2020). Compared to mature PSII, twelve residues of the D1 C-terminal tail must undergo significant conformational changes to bridge the side chains of Glu333, His337 and Asp342, as well as to bring the C-terminus of Ala344 in the correct position to coordinate the Mn4CaO5 cluster ( Fig.…”

Section: Discussioncontrasting

confidence: 46%

“…Previous structural studies aimed to obtain mechanistic insights into the dark-rearrangement by removing the Mn4CaO5 cluster from fully assembled PSII, either by depleting it directly from PSII crystals by chemical treatment (Zhang et al, 2017) or by cryo-EM single particle analysis in manganese-and calcium-free buffer (Gisriel et al, 2020). The X-ray structure was indeed missing the Mn4CaO5 cluster, but the D1 C-terminus followed mostly the same trajectory as found in the mature PSII-dimer structure.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the structure might be artificially stabilized by crystal packing forces. The cryo-EM structure, on the other hand, revealed a monomeric PSII that lacks extrinsic subunits and the Mn4CaO5 cluster (Gisriel et al, 2020). This structure is more similar to our PSII biogenesis intermediate PSII-I, as PsbY, PsbZ and PsbJ are also missing.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

How to build a water-splitting machine: structural insights into photosystem II assembly

Zabret

Bohn

Schuller

et al. 2020

Preprint

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Biogenesis of photosystem II (PSII), nature’s water splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the structure of such a PSII assembly intermediate with 2.94 Å resolution. It contains three assembly factors (Psb27, Psb28, Psb34) and provides detailed insights into their molecular function. Binding of Psb28 induces large conformational changes at the PSII acceptor side, which distort the binding pocket of the mobile quinone (QB) and replace bicarbonate with glutamate as a ligand of the non-heme iron, a structural motif found in reaction centers of non-oxygenic photosynthetic bacteria. These results reveal novel mechanisms that protect PSII from damage during biogenesis until water splitting is activated. Our structure further demonstrates how the PSII active site is prepared for the incorporation of the Mn4CaO5 cluster, which performs the unique water splitting reaction.One Sentence HighlightThe high-resolution Cryo-EM structure of the photosystem II assembly intermediate PSII-I reveals how nature’s water splitting catalyst is assembled, protected and prepared for photoactivation by help of the three assembly factors Psb27, Psb28 and Psb34.

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Section: Discussioncontrasting

confidence: 46%

Section: Discussionmentioning

confidence: 99%

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How to build a water-splitting machine: structural insights into photosystem II assembly

Zabret

Bohn

Schuller

et al. 2020

Preprint

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“…In comparison to other PSII structures, new knowledge on the assembly of the OEC from higher plants can possibly be derived from our model which exhibits similar characteristics to PSII still in assembly stage, prior to the binding of the extrinsic PsbP and PsbQ: the monomeric Synechocystis apo-PSII 40 presents analogous features to the high-resolution Arabidopsis PSII, particularly at the Mn4CaO5 binding-site.…”

Section: Discussionmentioning

confidence: 91%

“…The following steps are the oxidation of the first-bound Mn 2+ and the so-called 'dark rearrangement', proposed as a light-independent dynamic where the C-terminal of the D1 protein adopts a new structural conformation like the observed in the Mn4CaO5 binding pocket of mature PSII 39 . In an attempt to gain new information of this activation process, Gisriel and colleagues 40 isolated monomeric PSII from Synechocystis sp. PCC 6803 that were EDTA-washed and buffer exchanged.…”

Section: Introductionmentioning

confidence: 99%

High-resolution model of Arabidopsis Photosystem II reveals the consequences of digitonin-extraction

Graça

Hall

Persson

et al. 2021

Preprint

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In higher plants, the photosynthetic process is performed and regulated by Photosystem II (PSII). Arabidopsis thaliana was the first higher plant with a fully sequenced genome, conferring it the status of a model organism; nonetheless, a high-resolution structure of its Photosystem II is missing. We present the first Cryo-EM high-resolution structure of Arabidopsis PSII supercomplex with average resolution of 2.79 Å, an important model for future PSII studies. The digitonin extracted PSII complexes demonstrate the importance of: the LHG2630-lipid-headgroup in the trimerization of the light-harvesting complex II; the stabilization of the PsbJ subunit and the CP43-loop E by DGD520-lipid; the choice of detergent to maintain the integrity of membrane protein complexes. We propose that PsbW and PsbH subunits participate in the phospho-signalling dimerization of the complex, important to the assembly/repair processes of Photosystem II. Furthermore, our data shows at the anticipated Mn4CaO5-site a single metal ion density as a reminiscent early stage of PSII photoactivation.

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Synthesizing Mechanism of the Mn₄Ca Cluster Mimicking the Oxygen‐Evolving Center in Photosynthesis

Chen

Yao

et al. 2022

ChemSusChem

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The photosynthetic oxygen-evolving center (OEC) is a unique Mn 4 CaO 5 cluster that serves as a blueprint to develop superior water-splitting catalysts for the generation of solar fuels in artificial photosynthesis. It is a great challenge and longstanding issue to reveal the synthesizing mechanism of this Mn 4 CaO 5 cluster in both natural and artificial photosynthesis. Herein, efforts were made to reveal the synthesizing mechanism of an artificial Mn 4 CaO 4 cluster, a close mimic of the OEC. Four key intermediates were successfully isolated and structurally characterized for the first time. It was demonstrated that the Mn 4 CaO 4 cluster could be formed through a reaction between a thermodynamically stable Mn 3 CaO 4 cluster and an unusual fourcoordinated Mn III ion, followed by stabilization process through binding an organic base (e.g., pyridine) on the "dangling" Mn ion. These findings shed new light on the synthesizing mechanism of the OEC and rational design of new artificial water-splitting catalysts. Figure 4. Synthesizing mechanism of the Mn 4 CaO 4 cluster.

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Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex

Cited by 44 publications

References 92 publications

How to build a water-splitting machine: structural insights into photosystem II assembly

How to build a water-splitting machine: structural insights into photosystem II assembly

High-resolution model of Arabidopsis Photosystem II reveals the consequences of digitonin-extraction

Synthesizing Mechanism of the Mn₄Ca Cluster Mimicking the Oxygen‐Evolving Center in Photosynthesis

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Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex

Cited by 44 publications

References 92 publications

How to build a water-splitting machine: structural insights into photosystem II assembly

How to build a water-splitting machine: structural insights into photosystem II assembly

High-resolution model of Arabidopsis Photosystem II reveals the consequences of digitonin-extraction

Synthesizing Mechanism of the Mn4Ca Cluster Mimicking the Oxygen‐Evolving Center in Photosynthesis

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Synthesizing Mechanism of the Mn₄Ca Cluster Mimicking the Oxygen‐Evolving Center in Photosynthesis