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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

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Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
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Oxygenic Photosynthesis01:26

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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

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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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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
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Anoxygenic Photosynthesis01:30

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Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
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Updated: May 5, 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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P680(+) reduction in oxygen-evolving Photosystem II core complexes.

P B Lukins1, A Post, P J Walker

  • 1School of Physics, University of Sydney, 2006, NSW, Australia.

Photosynthesis Research
|November 26, 2013
PubMed
Summary
This summary is machine-generated.

Researchers investigated the speed of P680(+) reduction in spinach Photosystem II (PS II) using advanced spectroscopy. They identified new kinetic components, suggesting altered interactions at the water-splitting site, crucial for photosynthesis.

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Area of Science:

  • Photosynthesis research
  • Plant biochemistry
  • Spectroscopy

Background:

  • Photosystem II (PS II) is central to oxygenic photosynthesis.
  • Understanding electron transfer kinetics in PS II is key to elucidating its function.
  • The P680(+) reduction kinetics are influenced by the water-splitting complex.

Purpose of the Study:

  • To determine the kinetics of P680(+) reduction in spinach PS II core particles.
  • To identify and characterize transient species and electron transfer pathways.
  • To investigate the role of the water-splitting catalytic site in these kinetics.

Main Methods:

  • Utilized repetitive and single-flash 830 nm transient absorption spectroscopy.
  • Studied PS II core particles with turnover blocked and under normal conditions.
  • Analyzed data using amplitude and kinetic analysis of flash dependence.

Main Results:

  • Estimated radical-pair lifetimes of 2 ns and 19 ns when PS II turnover is blocked.
  • Observed decay times of 7 ns, 40 ns, and 95 ns in nanosecond measurements.
  • Identified a 7 ns component suggesting modified interactions at the water-splitting site.
  • Measured microsecond decay times of 4 μs and 90 μs, assigning the latter to P680(+)-QA(-) recombination.

Conclusions:

  • The 40 ns and 95 ns components align with S-state controlled Yz → P680(+) electron transfer.
  • The 7 ns component provides evidence for an additional process linked to the water-splitting site.
  • The 4 μs component's origin is linked to the water-splitting center, while 90 μs is P680(+)-QA(-) recombination.
  • Kinetic analysis supports the current model of the oxygen-evolving complex.