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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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The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.5K
Photosystems01:32

Photosystems

4.8K
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...
4.8K
The Photochemical Reaction Center01:29

The Photochemical Reaction Center

4.1K
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...
4.1K
Photosystem II01:22

Photosystem II

70.0K
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...
70.0K
Structure of Porins01:21

Structure of Porins

2.9K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
2.9K

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Cryo-EM structure of photosystem II supercomplex from a green microalga with extreme phototolerance.

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A unique light-harvesting complex protein family, LHCE, is involved in far-red absorption by photosystems I and II in Euglena gracilis.

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Related Experiment Video

Updated: Jun 8, 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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Unique structural attributes of the PSI-NDH supercomplex in Physcomitrium patens.

Monika Opatíková1, Roman Kouřil1

  • 1Department of Biophysics, Faculty of Science, Palacký University, Olomouc, Czech Republic.

The Plant Journal : for Cell and Molecular Biology
|November 3, 2024
PubMed
Summary

The moss Physcomitrium patens exhibits flexible Photosystem I (PSI)-NADH dehydrogenase-like complex (NDH) supercomplex formation, revealing early evolutionary adaptations in plant photosynthesis. This adaptability contrasts with the more rigid structures found in flowering plants.

Keywords:
LHCA5PSI‐NDH supercomplexPhyscomitrium patenscyclic electron transportsingle particle analysistransmission electron microscopy

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Area of Science:

  • Plant molecular biology
  • Photosynthesis research
  • Evolutionary botany

Background:

  • Cyclic electron transport around Photosystem I (PSI) protects plants under varying light.
  • Proton Gradient Regulation 5 protein/Proton Gradient Regulation 5-like photosynthetic phenotype 1 protein (PGR5/PGRL1) and NADH dehydrogenase-like complex (NDH) mediate this process.
  • Angiosperm NDH complexes interact with two PSI units via LHCA5 and LHCA6 antennae for stability.

Purpose of the Study:

  • To investigate the evolutionary origins of the PSI-NDH supercomplex.
  • To provide structural evidence for PSI-NDH supercomplex formation in the moss Physcomitrium patens (Pp).
  • To understand the structural flexibility and adaptive mechanisms at the PSI-NDH interface.

Main Methods:

  • Single particle electron microscopy was used to determine the structure of the Pp PSI-NDH supercomplex.
  • Comparative analysis of structural configurations in Pp versus angiosperms.

Main Results:

  • Physcomitrium patens forms a PSI-NDH supercomplex with a unique ability to bind a single PSI in two distinct configurations.
  • One configuration resembles the angiosperm model, while the other shows a novel, rotated PSI orientation.
  • This flexibility is attributed to variable LHCA5 incorporation, indicating early evolutionary adaptation.

Conclusions:

  • The structural flexibility in Pp's PSI-NDH supercomplex highlights an early evolutionary adaptation for photosynthetic diversity.
  • This variability appears to have decreased with increasing structural complexity in vascular plants.
  • The study clarifies the evolutionary trajectory of PSI-NDH supercomplexes and emphasizes the dynamic nature of photosynthetic adaptation.