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Related Concept Videos

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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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Related Experiment Video

Updated: Jun 2, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Solid-state NMR and functional studies on proteorhodopsin.

Nicole Pfleger1, Andreas C Wörner, Jun Yang

  • 1Institute for Biophysical Chemistry, Goethe University Frankfurt, Max von Laue Str. 9, 60438 Frankfurt/M., Germany.

Biochimica Et Biophysica Acta
|March 10, 2009
PubMed
Summary

Proteorhodopsins (PR) in marine bacteria function as light-driven proton pumps, potentially harnessing energy. Their properties, including proton transfer and environmental pH adaptation, are explored using advanced NMR techniques.

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Area of Science:

  • Microbiology
  • Biophysics
  • Structural Biology

Background:

  • Proteorhodopsins (PR) are abundant in marine bacteria, exhibiting environmental color tuning.
  • Certain PR species function as light-driven proton pumps, suggesting roles in energy generation and pH regulation.

Purpose of the Study:

  • To review and summarize recent findings on proteorhodopsin function and structure.
  • To investigate proton transfer mechanisms and the role of bound water using biophysical techniques.
  • To analyze the impact of mutations on PR chromophore properties.

Main Methods:

  • Fluorescence assays to demonstrate in vitro proton transfer.
  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy, including 2D (13)C-(13)C DARR and (15)N-(1)H HETCOR MAS NMR.
  • Site-directed mutagenesis to study conserved residues.

Main Results:

  • Proton transfer by PR in vitro is pH-dependent and vectorial.
  • Solid-state NMR revealed bound water near the protonated Schiff base, potentially aiding proton transfer.
  • Mutations at conserved residue H75 significantly altered optical absorption and pK(a) but minimally affected Schiff base NMR shifts.

Conclusions:

  • Proteorhodopsins play a significant role in marine microbial energy transduction.
  • Bound water molecules are implicated in the proton transfer mechanism of PR.
  • Conserved residues like H75 are crucial for tuning PR's photophysical and biochemical properties.