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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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Plants and other photosynthetic organisms comprise pigments capable of absorption of direct sunlight. These pigments are present in the reaction center - the main site of photochemical reactions as well as in the antenna complex. Under average light conditions, the rate at which reaction center pigments absorb light is far below the electron transport chain's capacity. As a result, the reaction center alone cannot provide enough energy to drive photosynthesis. The photosynthetic efficiency can...
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Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
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Related Experiment Video

Updated: Apr 28, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Bacteriorhodopsin: Would the real structural intermediates please stand up?

Cecilia Wickstrand1, Robert Dods1, Antoine Royant2

  • 1Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.

Biochimica Et Biophysica Acta
|June 12, 2014
PubMed
Summary
This summary is machine-generated.

Bacteriorhodopsin (bR) proton pump structural changes upon illumination are reproducible across studies. Analysis reveals consistent movements in helices and water molecules, clarifying the light-driven mechanism.

Keywords:
BacteriorhodopsinGlobal structural analysisProton pumpingStructural intermediates

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Area of Science:

  • Structural biology
  • Biophysics
  • Membrane protein research

Background:

  • Bacteriorhodopsin (bR) is a well-studied light-driven proton pump.
  • Extensive structural data (X-ray, electron diffraction, NMR) are available in the Protein Data Bank.
  • Previous studies examined light-induced, mutation-induced, and pH-dependent structural changes.

Purpose of the Study:

  • To identify reliable light-induced structural changes in bR by analyzing deposited structural data.
  • To develop a unified understanding of the bR proton pumping mechanism based on reproducible structural observations.

Main Methods:

  • Internal distance matrix analysis to hierarchically cluster bR structures.
  • Difference Fourier analysis of deposited X-ray diffraction data.
  • Comparison of structures across multiple independent studies.

Main Results:

  • Internal distance matrix analysis separated structures by crystal form, highlighting crystallization influence.
  • Eleven studies of illuminated bR crystals clustered, showing reproducible helix movements (C towards G, F away from A/B/G).
  • Consistent negative difference density at Wat402 (involved in retinal Schiff Base H-bonding) and reproducible side-chain/water displacements were observed.

Conclusions:

  • Reproducible structural changes in bR upon illumination provide a unified view of the proton pumping mechanism.
  • Crystallization conditions significantly influence bR structure.
  • X-ray radiation damage affects Wat402 and key aspartate residues (Asp85, Asp212).