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Related Concept Videos

Photosystem II01:22

Photosystem II

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The multi-protein complex photosystem II (PS II) harvests photons and transfers their energy through its bound pigments to its reaction center, and ultimately to photosystem I (PSI) through the electron transport chain. The pigments responsible for caputirng the light energy in photosystems include chlorophyll a, chlorophyll b, and carotenoids.
The pigment molecules are arranged across  two photosystem domains — the antenna complex and the reaction center. The main aim of the pigment...
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Photosystem I01:27

Photosystem I

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Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
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Photosystems01:32

Photosystems

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Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment...
5.8K
The Photochemical Reaction Center01:29

The Photochemical Reaction Center

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Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
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The Antenna Complex01:15

The Antenna Complex

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Plants and other photosynthetic organisms comprise pigments capable of absorption of direct sunlight. These pigments are present in the reaction center - the main site of photochemical reactions as well as in the antenna complex. Under average light conditions, the rate at which reaction center pigments absorb light is far below the electron transport chain's capacity. As a result, the reaction center alone cannot provide enough energy to drive photosynthesis. The photosynthetic efficiency can...
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The Z-Scheme of Electron Transport in Photosynthesis01:34

The Z-Scheme of Electron Transport in Photosynthesis

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The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
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Related Experiment Video

Updated: Nov 9, 2025

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
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Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues

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Structural insights into photosystem II assembly.

Jure Zabret1, Stefan Bohn2, Sandra K Schuller3,4

  • 1Department of Plant Biochemistry, Faculty of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.

Nature Plants
|April 13, 2021
PubMed
Summary
This summary is machine-generated.

Researchers used cryo-electron microscopy to reveal how auxiliary proteins assist in photosystem II (PSII) assembly. This structure explains how PSII is protected during biogenesis before water splitting begins.

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A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Photosynthesis Research

Background:

  • Photosystem II (PSII) is crucial for oxygenic photosynthesis, acting as nature's water-splitting catalyst.
  • The assembly of functional PSII requires assistance from various protein factors to ensure proper structure and function.
  • Understanding PSII biogenesis is key to comprehending the evolution and optimization of photosynthetic processes.

Purpose of the Study:

  • To elucidate the structural basis of PSII assembly intermediates.
  • To characterize the molecular functions of key assembly factors (Psb27, Psb28, Psb34) during PSII biogenesis.
  • To reveal protective mechanisms employed during PSII assembly before water-splitting capability is established.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the high-resolution structure of a PSII assembly intermediate.
  • Structural analysis focused on the interactions between PSII core components and associated assembly factors.
  • Comparative structural analysis with other photosynthetic reaction centers was performed.

Main Results:

  • A high-resolution (2.94 Å) structure of a Thermosynechococcus elongatus PSII assembly intermediate containing Psb27, Psb28, and Psb34 was obtained.
  • Psb28 binding was shown to induce significant conformational changes at the PSII acceptor side, affecting the quinone (QB) binding pocket.
  • A structural motif involving glutamate, typically found in non-oxygenic photosynthetic bacteria, was observed, suggesting a protective role during assembly.

Conclusions:

  • The study reveals novel mechanisms protecting PSII from photodamage during its assembly phase, prior to the activation of water splitting.
  • The structure provides insights into the precise preparation of the PSII active site for the subsequent incorporation of the Mn4CaO5 cluster.
  • This work advances our understanding of the intricate process of PSII biogenesis and its regulation.