Charge transport in proteins probed by resonant photoemission

Phys Rev Lett. 2009 Mar 6;102(9):098101. doi: 10.1103/PhysRevLett.102.098101. Epub 2009 Mar 5.

Abstract

The degrees of charge localization in the highest occupied and lowest unoccupied molecular orbitals (HOMO and LUMO) of the bacterial surface layer protein of Bacillus sphaericus NCTC 9602 were studied by resonant photoemission. In agreement with a charge transport hopping mechanism that involves torsional motions of the peptide backbone, the lifetime of electrons excited into the LUMO was found to be approximately 100 fs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / chemistry
  • Bacillus / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / metabolism
  • Models, Molecular
  • Spectrometry, X-Ray Emission / methods

Substances

  • Bacterial Proteins
  • Membrane Glycoproteins
  • S-layer proteins