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Ultrafast, remote-controlled protonation reaction enables structural changes in a phytochrome.

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Photoactive proteins use a novel proton transfer mechanism. A conserved histidine residue relays photoexcitation, enabling rapid signal transduction within the protein matrix.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Photochemistry

Background:

  • Photoactive proteins rely on precise chromophore-protein interactions.
  • Proton transfer reactions, like proton-coupled electron transfer, are known coupling mechanisms.
  • Undiscovered proton dislocation mechanisms may exist.

Purpose of the Study:

  • To investigate the mechanism of photoexcitation energy transfer in phytochrome.
  • To elucidate novel proton transfer pathways in photoactive proteins.
  • To understand how photoexcitation signals are transduced within protein matrices.

Main Methods:

  • Femtosecond crystallography to capture dynamic structural changes.
  • Molecular modeling to simulate and interpret observed rearrangements.
  • Femtosecond infrared spectroscopy for independent confirmation of proton dynamics.

Main Results:

  • A femtosecond movie revealed a space-conserving D-ring rotation in the excited state.
  • Rearrangement of a hydrogen bond network occurred within 300 fs.
  • A protonation shift of histidine-260 was identified as the key event preceding chromophore isomerization.

Conclusions:

  • A 'remote-controlled' proton transfer mechanism involving histidine-260 was proposed.
  • This mechanism rapidly relays photoexcitation to the protein matrix.
  • This proton transfer pathway may be a widespread mechanism for signal transduction in enzymes.