通过共振光发射探测蛋白质中的电荷传输。
Charge transport in proteins probed by resonant photoemission.
作者信息
Vyalikh D V, Maslyuk V V, Blüher A, Kade A, Kummer K, Dedkov Yu S, Bredow T, Mertig I, Mertig M, Molodtsov S L
机构信息
Institut für Festkörperphysik, Technische Universität Dresden, D-01062 Dresden, Germany.
出版信息
Phys Rev Lett. 2009 Mar 6;102(9):098101. doi: 10.1103/PhysRevLett.102.098101. Epub 2009 Mar 5.
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.
通过共振光发射研究了球形芽孢杆菌NCTC 9602细菌表面层蛋白最高占据分子轨道和最低未占据分子轨道（HOMO和LUMO）中的电荷局域化程度。与涉及肽主链扭转运动的电荷传输跳跃机制一致，发现激发到LUMO中的电子寿命约为100飞秒。
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