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Related Concept Videos

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
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 Z-Scheme of Electron Transport in Photosynthesis01:34

The Z-Scheme of Electron Transport in Photosynthesis

10.0K
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...
10.0K
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 Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.5K
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
The Antenna Complex01:42

The Antenna Complex

6.0K
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...
6.0K

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Related Experiment Video

Updated: Jun 17, 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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Bidirectional Energy Flow in the Photosystem II Supercomplex.

Cristina Leonardo1,2, Shiun-Jr Yang2,3,4, Kaydren Orcutt2,3

  • 1Department of Chemistry, University of California, Berkeley, California 94720, United States.

The Journal of Physical Chemistry. B
|August 14, 2024
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Photosystem II (PSII) balances light harvesting and photoprotection. New research reveals how supercomplex interactions enable rapid energy dissipation, preventing damage from excess light and improving artificial solar devices.

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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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Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting
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Area of Science:

  • Photosynthesis research
  • Bioenergetics
  • Quantum biology

Background:

  • Photosystem II (PSII) in plants and algae must balance light harvesting with photoprotection under fluctuating light.
  • The energy landscape of PSII supercomplexes (PSII-SC) is complex, and individual components don't reveal combined functions.
  • Understanding PSII-SC energy dynamics is crucial for optimizing photosynthesis and artificial energy systems.

Purpose of the Study:

  • To investigate the energy transfer dynamics within the C2S2-type PSII supercomplex.
  • To elucidate how interactions between components lead to efficient light harvesting and photoprotection.
  • To provide a quantitative description of PSII-SC's dual functionality.

Main Methods:

  • Utilized two-dimensional electronic-vibrational (2DEV) spectroscopy for enhanced spectral resolution and real-space energy mapping.
  • Employed quantum dynamical simulations for kinetic modeling of 210 chromophores.
  • Combined spectroscopic and computational approaches to study energy transfer.

Main Results:

  • Identified emergent energy transfer pathways within the PSII-SC.
  • Demonstrated that excitation energy can transfer away from reaction centers faster than it transfers to them.
  • Showed that peripheral quenching centers effectively dissipate excess energy, preventing overexcitation.

Conclusions:

  • The PSII-SC's ability to manage excess light energy arises from specific interactions between its components.
  • This understanding is fundamental for improving artificial solar energy devices and bioengineering for crop yield.
  • The study provides quantitative insights into the complex functional integration within PSII-SC.