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Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

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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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UV–Vis Spectroscopy: Molecular Electronic Transitions01:16

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In Ultraviolet–Visible (UV–Vis) spectroscopy, the absorption of electromagnetic radiation is used to probe the electronic structure of molecules. This technique provides insights into molecular electronic transitions, particularly the movement of electrons between different molecular orbitals. Radiation is absorbed if the energy of the electromagnetic radiation passing through the molecule is precisely equal to the energy difference between the excited and ground states. During this...
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The absorbance of UV and visible (UV–visible) radiations is measured using a UV–visible spectrophotometer. Deuterium lamps, which emit UV radiation, and tungsten lamps, which produce radiation in the visible region, are used as light sources in UV–visible spectrophotometers. A monochromator or prism is used for diffraction grating, i.e., to split the incoming radiation into different wavelengths. A system of slits is used to focus the desired wavelength on the sample cell.
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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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A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR

Marvin Asido1,2, Gerrit H U Lamm1, Jonas Lienert1

  • 1Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, Max-von-Laue Straße 7, 60438, Frankfurt (Main), Germany.

Angewandte Chemie (International Ed. in English)
|November 11, 2024
PubMed
Summary
This summary is machine-generated.

Microbial rhodopsins use photoisomerization for function. Near-UV and mid-IR spectroscopy reveal retinal changes and ion interactions, detailing photocycle dynamics.

Keywords:
IR spectroscopyUV/Vis spectroscopyenergy conversionmicrobial rhodopsinsphotoisomerization

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Area of Science:

  • Biophysical Chemistry
  • Spectroscopy
  • Photochemistry

Background:

  • Isomerization of retinal is central to microbial rhodopsin function.
  • Understanding the dynamic interplay between protein structure and retinal relaxation is crucial.
  • Chromophore-specific markers are needed for time-resolved spectral analysis.

Purpose of the Study:

  • To investigate the dynamic interplay between protein structural changes and retinal thermal relaxation in microbial rhodopsins.
  • To utilize near-UV and mid-IR spectroscopy for chromophore-specific probing.
  • To analyze the photocycle dynamics of various microbial rhodopsin pumps (H+, Na+, Cl-).

Main Methods:

  • Systematic time-resolved spectroscopic study.
  • Utilized near-UV and mid-IR fingerprint regions.
  • Investigated H+- (HsBR, (G)PR), Na+- (KR2, ErNaR), and Cl-- (NmHR) pumps.

Main Results:

  • Near-UV spectroscopy effectively probes retinal configuration and transient ion binding.
  • Mid-IR spectroscopy provides insights into the fingerprint region.
  • Combined spectral analysis precisely describes retinal configurations throughout the photocycle.

Conclusions:

  • The near-UV region is sensitive to retinal configuration and electrostatic environment, including ion binding.
  • The combination of near-UV and mid-IR spectroscopy offers a powerful tool for detailed photocycle analysis.
  • This approach allows precise, time-resolved characterization of chromophore-charge interactions and protein dynamics.