Charge transport in proteins probed by resonant photoemission.
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.
Vyalikh
D V
DV
Institut für Festkörperphysik, Technische Universität Dresden, D-01062 Dresden, Germany.
Maslyuk
V V
VV
Blüher
A
A
Kade
A
A
Kummer
K
K
Dedkov
Yu S
YS
Bredow
T
T
Mertig
I
I
Mertig
M
M
Molodtsov
S L
SL
D001407:Bacillus / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D013052:Spectrometry, X-Ray Emission / Q000379:methods
D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; C055764:S-layer proteins