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Related Concept Videos

The Photochemical Reaction Center01:29

The Photochemical Reaction Center

5.9K
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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Channel Rhodopsins01:11

Channel Rhodopsins

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
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Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

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At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
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Anoxygenic Photosynthesis01:30

Anoxygenic Photosynthesis

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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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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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Articles linked to this work by shared authors, journal, and citation graph.

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Antimicrobial peptides containing arginine.

Biochemistry. Biokhimiia·2003
Same author

FTIR emission spectra of bacteriorhodopsin in a vibrational excited state.

Biochemistry. Biokhimiia·2001
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[Absorption of infrared radiation by a thin water layer].

Biofizika·2001
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[Investigation of the effects of dehydration on bacterial rhodopsin by laser resonance Raman spectroscopy].

Molekuliarnaia biologiia·1982
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Effect of water on the structure of bacteriorhodopsin and photochemical processes in purple membranes.

Biochimica et biophysica acta·1980
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[Picosecond flash photolysis of Halobacterium halobium bacteriorhodopsin at room and low temperatures].

Biofizika·1978

Related Experiment Video

Updated: Apr 11, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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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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[Photo-induced processes and reaction dynamics in bacteriorhodopsin].

E L Terpugov, O V Degtyareva

    Biofizika
    |May 29, 2015
    PubMed
    Summary

    This review explores photo-induced responses in bacteriorhodopsin, focusing on retinal-protein interactions. New spectroscopic data on amino acids reveal insights into the protein

    Area of Science:

    • Biophysics
    • Spectroscopy
    • Protein Chemistry

    Context:

    • Bacteriorhodopsin's photo-induced response mechanisms are not fully understood.
    • Retinal-protein interactions are crucial but remain obscure.
    • Observational advances are key to understanding these processes.

    Purpose:

    • To review advances in observing photo-induced responses in bacteriorhodopsin.
    • To elucidate the mechanisms of retinal-protein interactions.
    • To present new spectroscopic data on amino acids and their role.

    Summary:

    • This review discusses recent data on wild-type bacteriorhodopsin and model compounds.
    • New Fourier-transform infrared (FT-IR) emission spectroscopy data on amino acids are presented.
    • The study investigates the role of protein in primary processes using glycine and L-lysine as models.

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    Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
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    Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
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    Related Experiment Videos

    Last Updated: Apr 11, 2026

    Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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    Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
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    Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues

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    Impact:

    • Provides new spectroscopic insights into bacteriorhodopsin's photo-induced behavior.
    • Contributes to understanding the fundamental role of proteins in primary photochemical events.
    • Enhances knowledge of retinal-protein interactions in biological systems.