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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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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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Related Experiment Video

Updated: Feb 24, 2026

Determination of Photoreceptor Cell Spectral Sensitivity in an Insect Model from In Vivo Intracellular Recordings
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Surface Density-Dependent Interactions between Photoactivated Sensory Rhodopsin 2 and Its Transducer.

Tatsuya Sakamoto1, Jingyi Tang1, Soichiro Kato1

  • 1Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.

ACS Omega
|February 23, 2026
PubMed
Summary

Sensory rhodopsin 2 (pSRII) and its transducer (pHtrII) initiate signal transduction via membrane conformational changes, not HAMP domain interactions. This study reveals the primary mechanism of light signal transfer in this microbial photosensor system.

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Area of Science:

  • Microbiology
  • Biophysics
  • Structural Biology

Background:

  • Sensory rhodopsin 2 (pSRII) and its transducer (pHtrII) form a complex to regulate microbial flagellar rotation in response to light.
  • Previous studies suggest conformational changes in pSRII's F helix trigger pHtrII helix rotation, but the role of the HAMP domain in signal transduction remains unclear due to its flexibility.

Purpose of the Study:

  • To investigate the role of the HAMP domain in the protein-protein interactions and signal transduction between pSRII and pHtrII.
  • To elucidate the structural changes occurring in the pSRII-pHtrII complex under physiological membrane conditions.

Main Methods:

  • Surface-enhanced infrared spectroscopy (SEIR) was used to analyze structural changes in pSRII and pSRII fused with different domains of pHtrII (including or excluding the HAMP domain).
  • Experiments were conducted under physiological membrane orientation to mimic in vivo conditions.

Main Results:

  • The light-induced spectral changes in the amide I region of pSRII-pHtrII complexes were attenuated in a surface-density-dependent manner.
  • This attenuation was similar whether the HAMP domain was present or absent, indicating it does not significantly influence the conformational changes in the membrane region.

Conclusions:

  • The primary signal transduction from pSRII to pHtrII occurs through conformational changes within the membrane-bound regions of the complex.
  • The HAMP domain is not essential for the initial light-induced conformational changes mediating signal transfer between pSRII and pHtrII.