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Related Concept Videos

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

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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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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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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...
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Oxygenic Photosynthesis01:26

Oxygenic Photosynthesis

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Oxygenic photosynthesis is a fundamental process in which light energy is harnessed to drive the oxidation of water, leading to the production of molecular oxygen (O₂), adenosine triphosphate (ATP), and nicotinamide adenine dinucleotide phosphate (NADPH). This process is essential for sustaining aerobic life on Earth and is primarily carried out by cyanobacteria, algae, and plants. The core of oxygenic photosynthesis lies in the thylakoid membranes, where chlorophyll pigments facilitate...
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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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Conserved Structure, Altered Energetics: Iron-Sulfur Clusters in Visible and Far-Red Light Acclimated Photosystem I.

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Updated: Jan 11, 2026

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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Driving Electron Transfer in Photosystem I Using Far-Red Light: Overall Perspectives.

Jimit Patel1, Amen ElMasadef2, Abraham Peele Karlapudi3

  • 1Department of Chemistry, Brock University, St. Catharines, ON L2S 3A1, Canada.

Plants (Basel, Switzerland)
|November 13, 2025
PubMed
Summary
This summary is machine-generated.

Cyanobacteria adapt Photosystem I (PSI) to different light wavelengths by altering pigment structure and protein environment. This allows efficient electron transport and energy conversion across diverse light conditions.

Keywords:
FaRLiPPhotosystem Ielectron transfer reactionfar-red light photoacclimationfar-red photosynthesisreaction center

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Area of Science:

  • Biochemistry
  • Photosynthesis research
  • Structural biology

Background:

  • Photosystem I (PSI) is crucial for electron transfer in photosynthesis, producing NADPH.
  • Isolated PSI reaction centers (RCs) are explored for biohydrogen production.
  • Cyanobacteria exhibit diverse light utilization strategies for photosynthesis.

Purpose of the Study:

  • To review how different cyanobacteria species utilize varying light wavelengths for electron transport through PSI.
  • To analyze structural factors influencing PSI efficiency under different light conditions.
  • To compare PSI complexes from four cyanobacteria species with known atomic structures.

Main Methods:

  • Comparative analysis of atomic structures of PSI complexes from four cyanobacteria species.
  • Examination of electron transfer cofactors, pigment structure, and protein environments.
  • Investigation of hydrogen-bonding interactions within the PSI protein matrix.

Main Results:

  • Cyanobacteria like *T. elongatus* use chlorophyll *a* for visible light, while *H. hongdechloris* and *F. thermalis* produce chlorophyll *f* and *d* for red light.
  • *A. marina* consistently uses chlorophyll *d* for red light adaptation.
  • Structural differences in cofactors and protein environments tune absorption wavelengths and electron transfer energy levels.

Conclusions:

  • Cyanobacteria exhibit remarkable adaptability in PSI structure and function to optimize photosynthesis under different light spectra.
  • Interplay between pigment structure, protein environment, and hydrogen bonding is key to PSI efficiency and adaptability.
  • Understanding these adaptations can inform biohydrogen production and photosynthetic engineering.