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An electronic time scale in chemistry.

F Remacle1, R D Levine

  • 1The Fritz Haber Research Center for Molecular Dynamics, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|April 26, 2006
PubMed
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Ultrafast charge migration in peptides occurs in under a femtosecond, enabling real-time observation with attosecond electron removal. This phenomenon is particularly rapid in tyrosine-terminated tetrapeptides.

Area of Science:

  • Physical chemistry
  • Computational chemistry
  • Molecular dynamics

Background:

  • Ultrafast charge migration is a key process in molecular dynamics.
  • Selective bond dissociation after ionization has been experimentally observed.
  • Attosecond time-scale electron removal is necessary for real-time probing of charge migration.

Purpose of the Study:

  • To discuss ultrafast charge migration in small peptides.
  • To compare computational findings with experimental observations.
  • To explore the potential for real-time observation of charge migration.

Main Methods:

  • Computational studies of charge migration in peptides.
  • Comparison with experimental data on selective bond dissociation.
  • Theoretical modeling of electron dynamics on the attosecond timescale.

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Main Results:

  • Charge migration in tyrosine-terminated tetrapeptides occurs in less than 1 femtosecond.
  • Femtosecond pulses can observe slower relaxation due to electron spin correlation.
  • Ionizing deeper valence electrons indicates slower relaxation processes.
  • Charge migration along the peptide backbone is observed when a chromophoric amino acid is present.

Conclusions:

  • Attosecond time-resolved studies are crucial for understanding ultrafast charge migration.
  • Tyrosine-terminated tetrapeptides exhibit exceptionally rapid charge migration.
  • Site-selective ionization detection may be more feasible for tryptophan than tyrosine.