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Channel Rhodopsins

Channel Rhodopsins

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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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, whereas...

The Retina

The Retina

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Anatomy of the Eyeball

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G-Protein Gated Ion Channels

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GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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The Photochemical Reaction Center

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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: May 7, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Proteorhodopsin.

Christian Bamann¹, Ernst Bamberg¹, Josef Wachtveitl²

¹Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany.

Biochimica Et Biophysica Acta

|September 25, 2013

Summary

This summary is machine-generated.

Proteorhodopsins, abundant marine photoreceptors, exhibit unique molecular properties in their green-absorbing form. Their structure-function relationships offer insights into phototrophy and color tuning.

Keywords:

Charge transfer Electrophysiology NMR spectroscopy Photocycle Photoisomerization

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Area of Science:

Biochemistry
Molecular Biology
Marine Biology

Background:

Proteorhodopsins are abundant retinal-based photoreceptors in marine ecosystems.
Their phototrophic functions are crucial for understanding marine life.
The green-absorbing variant possesses unique molecular characteristics.

Purpose of the Study:

To describe the molecular properties of proteorhodopsins, focusing on the green-absorbing variant.
To elucidate the structure-function relationships within the proteorhodopsin family.
To highlight the biophysical understanding of green proteorhodopsin.

Main Methods:

Advanced spectroscopic methods.
Electrophysiological techniques.
Structural analysis of proteorhodopsin variants.

Main Results:

The green-absorbing proteorhodopsin shows a high pKa for its primary proton acceptor, stabilized by a conserved histidine.
A long-range interaction between the EF loop and chromophore influences color tuning.
Variable proton pumping vectoriality with complex voltage-dependence was observed.

Conclusions:

Proteorhodopsins exemplify profound structure-function relationships.
Green proteorhodopsin's biophysical understanding showcases combined spectroscopic and electrophysiological approaches.
Further research into proteorhodopsins can reveal novel phototrophic mechanisms.