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Related Experiment Videos

Subsecond proton-hole propagation in bacteriorhodopsin.

Bettina Schätzler1, Norbert A Dencher, Joerg Tittor

  • 1Laser Laboratory for Fast Reactions in Biology, Department of Biochemistry, Tel Aviv University, Israel.

Biophysical Journal
|January 14, 2003
PubMed
Summary

Proton transfer dynamics in bacteriorhodopsin were studied. A slow proton release process, creating a "proton hole," was identified as rate-limiting, influencing equilibrium recovery.

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Area of Science:

  • Biophysics
  • Photochemistry
  • Membrane Protein Dynamics

Background:

  • Proton transfer is crucial for biological energy transduction.
  • Bacteriorhodopsin acts as a light-driven proton pump.
  • Understanding proton dynamics is key to elucidating protein function.

Purpose of the Study:

  • To investigate the proton balance between bacteriorhodopsin's Schiff base and the bulk phase.
  • To characterize the time-resolved proton transfer during the photocycle.
  • To identify rate-limiting steps in proton re-equilibration.

Main Methods:

  • Laser Induced Proton Pulse Method.
  • Time-resolved monitoring of bacteriorhodopsin photocycle and proton cycle.
  • Calculation of proton balance in the absence of buffer.

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Main Results:

  • A slow, subsecond relaxation of proton disequilibrium was observed after 1 ms.
  • The Schiff base reprotonates before full proton re-equilibration.
  • Protonation of Asp96 (D96) acts as a slow, rate-limiting step, creating a "proton hole".

Conclusions:

  • The proton hole propagation is influenced by ionic strength and charged residue modifications.
  • Slow proton transfer to D96 is a bottleneck in the proton cycle.
  • These findings offer insights into the mechanisms of proton transport in proteins.