Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Photochemical Reaction Center01:29

The Photochemical Reaction Center

4.2K
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...
4.2K
Channel Rhodopsins01:11

Channel Rhodopsins

2.6K
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,...
2.6K
Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

6.1K
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,...
6.1K
Photochemical Electrocyclic Reactions: Stereochemistry01:26

Photochemical Electrocyclic Reactions: Stereochemistry

1.9K
The absorption of UV–visible light by conjugated systems causes the promotion of an electron from the ground state to the excited state. Consequently, photochemical electrocyclic reactions proceed via the excited-state HOMO rather than the ground-state HOMO. Since the ground- and excited-state HOMOs have different symmetries, the stereochemical outcome of electrocyclic reactions depends on the mode of activation; i.e., thermal or photochemical.
Selection Rules: Photochemical Activation
1.9K
Photosystem I01:27

Photosystem I

63.0K
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...
63.0K
Photosystem II01:22

Photosystem II

71.1K
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...
71.1K

You might also read

Related Articles

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

Sort by
Same author

Different dimerization affinity and orientation of fluorescent proteins eGFP and eYFP.

Physical chemistry chemical physics : PCCP·2026
Same author

Amino acid deaminase outperforms transaminase in α-keto acid production from amino acids.

Metabolic engineering·2026
Same author

Linking Clinical and Environmental Multidrug Resistance Plasmids Captured from the Tama River Flowing Through the Tokyo Megalopolis.

Antibiotics (Basel, Switzerland)·2026
Same author

Contribution of Fat-Signaling and Crumbs-Expanded Modules to Exaggerated Growth of Weaponized Mandible in a Stag Beetle and Its Evolutionary Implications.

Zoological science·2026
Same author

Kinetic Insights into Photoinduced Monomer-Dimer Conversion and Activation of Orange Carotenoid Protein.

The journal of physical chemistry. B·2026
Same author

Comparison of Predatory Phenotypes and Genotypes Between Bdellovibrio sp. BIS2 and Bacteriovorax sp. HI3 Isolated From the Same Freshwater Environment.

Environmental microbiology·2026

Related Experiment Video

Updated: Jul 19, 2025

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
06:26

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria

Published on: November 10, 2021

4.0K

Conformational change in an engineered biliverdin-binding cyanobacteriochrome during the photoconversion process.

Yuka Takeda1, Itsuki Ohtsu1, Takahisa Suzuki2

  • 1Graduate School of Science and Technology, Shizuoka University, 836 Ohya, Suruga, Shizuoka, 422-8529, Japan.

Archives of Biochemistry and Biophysics
|August 7, 2023
PubMed
Summary

Cyanobacteriochromes (CBCRs) are light-sensitive proteins. This study reveals that their photoconversion involves surface charge changes and α-helix modifications, not altered oligomeric states, aiding optogenetic tool development.

Keywords:
Circular dichroism spectroscopyNative PAGEOptogeneticsSize-exclusion chromatographyThermal relaxation

More Related Videos

Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis
08:07

Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis

Published on: September 11, 2018

15.4K
In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
11:55

In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae

Published on: October 10, 2014

18.3K

Related Experiment Videos

Last Updated: Jul 19, 2025

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
06:26

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria

Published on: November 10, 2021

4.0K
Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis
08:07

Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis

Published on: September 11, 2018

15.4K
In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
11:55

In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae

Published on: October 10, 2014

18.3K

Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Cyanobacteriochromes (CBCRs) are photoreceptors related to phytochromes, featuring diverse GAF domains.
  • Biliverdin (BV)-binding CBCR GAF domains are crucial for optogenetics due to BV's properties and far-red light absorption.
  • Typical BV-binding CBCR GAF domains undergo reversible photoconversion between distinct states.

Purpose of the Study:

  • To elucidate the conformational changes underlying the photoconversion process in BV-binding CBCR GAF domains.
  • To investigate potential alterations in oligomeric state, surface charge, and secondary structures during photoconversion.
  • To identify the specific regions involved in the conformational dynamics.

Main Methods:

  • Biochemical and spectral analyses were employed to study CBCR GAF domain photoconversion.
  • Protease digestion combined with mass spectrometry was used to pinpoint conformational change regions.
  • Oligomeric state, surface charge, and α-helix structural modifications were assessed.

Main Results:

  • No changes in the oligomeric state of the CBCR GAF domains were observed during photoconversion.
  • Photoconversion was associated with alterations in surface charge and modifications within α-helix structures.
  • Mass spectrometry and protease digestion identified specific regions undergoing conformational changes.

Conclusions:

  • The photoconversion of BV-binding CBCR GAF domains involves surface charge and α-helix structural rearrangements, not changes in oligomeric state.
  • These findings provide critical insights into the molecular mechanisms of CBCR function.
  • The identified conformational changes offer valuable information for the future design and optimization of optogenetic tools.