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Related Concept Videos

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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.
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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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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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Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
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Related Experiment Video

Updated: Jan 11, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Structural insights into an inward proton-pumping rhodopsin.

Jessica E Besaw1, Shiyun Peng1, Anling Kuo1

  • 1Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.

Biophysical Journal
|November 13, 2025
PubMed
Summary

The crystal structure of Antarctic rhodopsin (AntR), an inward proton pump, reveals unique features like a long C-terminal helix. This finding advances understanding of schizorhodopsin (SzR) proton transport mechanisms.

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A Rhodopsin Transport Assay by High-Content Imaging Analysis
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Area of Science:

  • Structural biology
  • Biochemistry
  • Microbial rhodopsins

Background:

  • Microbial rhodopsins facilitate light-driven proton transport.
  • Inward proton pumps, like xenorhodopsins (XeRs) and schizorhodopsins (SzRs), are less structurally characterized than outward pumps.
  • Limited structural data hinders understanding of inward proton pump variations.

Purpose of the Study:

  • To determine the crystal structure of Antarctic rhodopsin (AntR), a representative schizorhodopsin (SzR).
  • To elucidate the structural basis of inward proton transport in SzRs.
  • To compare AntR structure with other microbial rhodopsins.

Main Methods:

  • X-ray crystallography of AntR under acidic and basic conditions.
  • Structural analysis comparing AntR to known rhodopsin structures.
  • Functional analysis involving truncation of the C-terminal helix.

Main Results:

  • The AntR structure reveals short transmembrane helices and large cavities, similar to SzR4 but distinct from NsXeR and BcXeR.
  • A unique long C-terminal α-helix in AntR covers the cytoplasmic proton pathway.
  • Truncation of this helix reduced inward proton-pumping efficiency.
  • AntR exhibits pH-dependent retinal configuration.

Conclusions:

  • The AntR structure provides crucial insights into the conserved and unique features of SzRs.
  • A putative inward proton transport mechanism for AntR is proposed based on structural and functional data.
  • Structural variations among inward proton pumps, including AntR, are highlighted.