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Updated: Jul 10, 2026

Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy
Published on: June 23, 2016
Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster
Ziyu Zhao1,2, Irene Vercellino1,3, Julian P Whitelegge4
1Institute of Science and Technology Austria, Klosterneuburg, Austria.
Researchers reveal structures of photosystem II (PSII) intermediates, uncovering how the oxygen-evolving complex assembles and disassembles. This provides insights into photosynthesis regulation and repair mechanisms in cyanobacteria.
Area of Science:
- Biochemistry
- Structural Biology
- Photosynthesis Research
Background:
- Oxygenic photosynthesis relies on the precise assembly and repair of photosystem II (PSII).
- Previous structural studies of PSII intermediates often used deletion mutants or in vitro subunit removal.
- Understanding PSII assembly is crucial for efficient energy conversion and cellular repair.
Purpose of the Study:
- To determine the high-resolution structures of naturally occurring dimeric PSII assembly/disassembly intermediates.
- To elucidate the mechanism of oxygen-evolving complex (OEC) assembly and disassembly.
- To investigate the role of extrinsic proteins and D1 subunit restructuring in PSII regulation.
Main Methods:
- Cryo-electron microscopy (cryo-EM) at approximately 2.2 Å resolution.
- Analysis of naturally occurring dimeric PSII intermediates from Thermosynechococcus vestitus.
- Integration of mass spectrometry data.
Main Results:
- Reported cryo-EM structures of inactive and semi-active dimeric PSII intermediates.
- Revealed a mechanism coordinating Mn4CaO5 cluster assembly/disassembly with extrinsic protein binding/release.
- Identified potential damage in inactive PSII complexes involving oxidized D1-His332.
Conclusions:
- The C-terminal tail of the D1 subunit plays a key role in regulating PSII assembly and disassembly.
- Conformational changes in D2, CP47, and CP43 are triggered by D1 restructuring.
- Structural insights into PSII repair mechanisms and potential damage pathways.
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