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Related Concept Videos

Channel Rhodopsins01:11

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.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

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...
Anatomy of the Eyeball01:20

Anatomy of the Eyeball

The eye is a spherical, hollow structure composed of three tissue layers. The outer layer — the fibrous tunic, comprises the sclera — a white structure — and the cornea, which is transparent. The sclera encompasses some of the ocular surface, most of which is not visible. However, the 'white of the eye' is distinctively visible in humans compared to other species. The cornea, a clear covering at the front of the eye, enables light penetration. The eye's middle layer, the vascular tunic,...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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.
Sensory organs,...
The Retina01:32

The Retina

The retina is a layer of nervous tissue at the back of the eye that transduces light into neural signals. This process, called phototransduction, is carried out by rod and cone photoreceptor cells in the back of the retina.
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

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Related Experiment Video

Updated: Jul 5, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis
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A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

Proteorhodopsins: an array of physiological roles?

Jed A Fuhrman1, Michael S Schwalbach, Ulrich Stingl

  • 1Department of Biological Sciences and Wrigley Institute, University of Southern California, Los Angeles, California 90089-0371, USA. fuhrman@usc.edu

Nature Reviews. Microbiology
|May 14, 2008
PubMed
Summary
This summary is machine-generated.

Marine bacteria and archaea possess diverse proteorhodopsins, challenging the idea that only chlorophyll captures solar energy. These proteins may have varied physiological functions beyond energy production.

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

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Last Updated: Jul 5, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

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Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
11:08

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Published on: December 7, 2021

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

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

Published on: June 27, 2014

Area of Science:

  • Microbiology
  • Marine Biology
  • Biochemistry

Background:

  • Metagenomic analyses reveal widespread proteorhodopsins in marine bacteria and archaea.
  • Proteorhodopsins are retinal-binding proteins similar to archaeal bacteriorhodopsins.
  • This challenges the exclusive role of chlorophyll in marine primary energy capture.

Purpose of the Study:

  • To investigate the energetic role and diverse physiological functions of marine proteorhodopsins.
  • To explore how proteorhodopsins contribute to energy transduction in marine microbial communities.

Main Methods:

  • Metagenomic analysis to identify and characterize proteorhodopsin diversity.
  • Comparative structural and functional analysis with known rhodopsins.
  • Experimental investigations into proteorhodopsin activity and physiological roles.

Main Results:

  • Widespread distribution of diverse proteorhodopsins found in marine bacteria and archaea.
  • Structural and functional similarities noted with archaeal bacteriorhodopsins, suggesting proton pumping.
  • Emerging evidence indicates a broader range of physiological functions beyond energy generation.

Conclusions:

  • Proteorhodopsins represent a significant, previously underappreciated energy source in marine ecosystems.
  • The functions of proteorhodopsins extend beyond simple light-driven proton pumping.
  • Further research is needed to fully elucidate the diverse roles of these proteins in marine microbial life.